Journal articles: 'HIV Receptors'

1

Shimizu, Nobuaki, Atsushi Tanaka, Atsushi Oue, Takahisa Mori, Chatchawann Apichartpiyakul, and Hiroo Hoshino. "A short amino acid sequence containing tyrosine in the N-terminal region of G protein-coupled receptors is critical for their potential use as co-receptors for human and simian immunodeficiency viruses." Journal of General Virology 89, no. 12 (December 1, 2008): 3126–36. http://dx.doi.org/10.1099/vir.0.2008/002188-0.

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Various G protein-coupled receptors (GPCRs) have the potential to work as co-receptors for human and simian immunodeficiency virus (HIV/SIV). HIV/SIV co-receptors have several tyrosines in their extracellular N-terminal region (NTR) as a common feature. However, the domain structure of the NTR that is critical for GPCRs to have co-receptor activity has not been identified. Comparative studies of different HIV/SIV co-receptors are an effective way to clarify the domain. These studies have been carried out only for the major co-receptors, CCR5 and CXCR4. A chemokine receptor, D6, has been shown to mediate infection of astrocytes with HIV-1. Recently, it was also found that an orphan GPCR, GPR1, and a formyl peptide receptor, FPRL1, work as potent HIV/SIV co-receptors in addition to CCR5 and CXCR4. To elucidate more about the domain of the NTR critical for HIV/SIV co-receptor activity, this study analysed the effects of mutations in the NTR on the co-receptor activity of D6, FPRL1 and GPR1 in addition to CCR5. The results identified a number of tyrosines that are indispensable for the activity of these co-receptors. The number and positions of those tyrosines varied among co-receptors and among HIV-1 strains. Moreover, it was found that a small domain of a few amino acids containing a tyrosine is critical for the co-receptor activity of GPR1. These findings will be useful in elucidating the mechanism that allows GPCRs to have the potential to act as HIV/SIV co-receptors.

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Garzino-Demo, Alfredo, and Robert C. Gallo. "HIV receptors on lymphocytes." Current Opinion in Hematology 10, no. 4 (July 2003): 279–83. http://dx.doi.org/10.1097/00062752-200307000-00005.

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3

Broder, Christopher C., and Ronald G. Collman. "Chemokine receptors and HIV." Journal of Leukocyte Biology 62, no. 1 (July 1997): 20–29. http://dx.doi.org/10.1002/jlb.62.1.20.

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Freeman, Tracey L., and Talia H. Swartz. "Purinergic Receptors: Elucidating the Role of these Immune Mediators in HIV-1 Fusion." Viruses 12, no. 3 (March 7, 2020): 290. http://dx.doi.org/10.3390/v12030290.

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Purinergic receptors are inflammatory mediators activated by extracellular nucleotides released by dying or injured cells. Several studies have described an important role for these receptors in HIV-1 entry, particularly regarding their activity on HIV-1 viral membrane fusion. Several reports identify purinergic receptor antagonists that inhibit HIV-1 membrane fusion; these drugs are suspected to act through antagonizing Env-chemokine receptor interactions. They also appear to abrogate activity of downstream mediators that potentiate activation of the NLRP3 inflammasome pathway. Here we review the literature on purinergic receptors, the drugs that inhibit their function, and the evidence implicating these receptors in HIV-1 entry.

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Jotwani, R., M. Muthukuru, and C. W. Cutler. "Increase in HIV Receptors/Co-receptors/α-defensins in Inflamed Human Gingiva." Journal of Dental Research 83, no. 5 (May 2004): 371–77. http://dx.doi.org/10.1177/154405910408300504.

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Transmission of HIV-1 through the oral cavity is considered to be a rare event. To identify factors in resistance/susceptibility to oral HIV-1 infection, we analyzed expression in human gingiva of HIV-1 receptors Langerin, DC-SIGN, MR, and GalCer, HIV-1 co-receptors CCCR5, CXCR4, and anti-microbial protein α-defensin-1. Our results show that healthy gingiva is infiltrated with cells expressing all HIV-1 receptors tested; however, there are very few CCR5+ cells and a complete absence of CXCR4+ cells in the lamina propria. In chronic periodontitis (CP), DC-SIGN, MR, CXCR4, and CCR5 increase, but this was accompanied by a ten-fold increase in α-defensin-1 mRNA. The CCR5+ cells were revealed to be T-cells, macrophages, and dermal dendritic cells. Moreover, epithelial expression of GalCer and CXCR4 together was not apical and showed no trend with underlying inflammation. Thus, low expression of HIV-1 co-receptors in health and high expression of α-defensin during CP may comprise endogenous factors that provide protection from oral HIV-1 infection.

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6

Turville, Stuart G., Jim Arthos, Kelli Mac Donald, Garry Lynch, Hassan Naif, Georgina Clark, Derek Hart, and Anthony L. Cunningham. "HIV gp120 receptors on human dendritic cells." Blood 98, no. 8 (October 15, 2001): 2482–88. http://dx.doi.org/10.1182/blood.v98.8.2482.

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Abstract Dendritic cells (DCs) are important targets for human immunodeficiency virus (HIV) because of their roles during transmission and also maintenance of immune competence. Furthermore, DCs are a key cell in the development of HIV vaccines. In both these settings the mechanism of binding of the HIV envelope protein gp120 to DCs is of importance. Recently a single C-type lectin receptor (CLR), DC-SIGN, has been reported to be the predominant receptor on monocyte-derived DCs (MDDCs) rather than CD4. In this study a novel biotinylated gp120 assay was used to determine whether CLR or CD4 were predominant receptors on MDDCs and ex vivo blood DCs. CLR bound more than 80% of gp120 on MDDCs, with residual binding attributable to CD4, reconfirming that CLRs were the major receptors for gp120 on MDDCs. However, in contrast to recent reports, gp120 binding to at least 3 CLRs was observed: DC-SIGN, mannose receptor, and unidentified trypsin resistant CLR(s). In marked contrast, freshly isolated and cultured CD11c+ve and CD11c−ve blood DCs only bound gp120 via CD4. In view of these marked differences between MDDCs and blood DCs, HIV capture by DCs and transfer mechanisms to T cells as well as potential antigenic processing pathways will need to be determined for each DC phenotype.

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Doepper, S., L. Kacani, B. Falkensammer, M. Dierich, and H. Stoiber. "Complement Receptors in HIV Infection." Current Molecular Medicine 2, no. 8 (December 1, 2002): 703–11. http://dx.doi.org/10.2174/1566524023361826.

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8

Doms, Robert W. "Fusing HIV and Chemokine Receptors." Journal of Immunology 186, no. 11 (May 19, 2011): 6073–75. http://dx.doi.org/10.4049/jimmunol.1100982.

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9

Weiss, Robin A. "HIV Receptors and Cellular Tropism." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 53, no. 4-5 (April 1, 2002): 201–5. http://dx.doi.org/10.1080/15216540212652.

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10

Jiang, Shibo. "HIV-1 — co-receptors binding." Nature Medicine 3, no. 4 (April 1, 1997): 367–68. http://dx.doi.org/10.1038/nm0497-367.

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11

Heredia, A., A. Vallejo, V. Soriano, J. S. Epstein, and I. K. Hewlett. "Chemokine receptors and HIV-2." AIDS 11, no. 9 (July 1997): 1198–99. http://dx.doi.org/10.1097/00002030-199709000-00025.

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12

Doms, Robert W. "Chemokine Receptors and HIV entry." AIDS 15 (February 2001): S34—S35. http://dx.doi.org/10.1097/00002030-200102001-00051.

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13

Speth, Cornelia, Laco Kacani, and Manfred R. Dierich. "Complement receptors in HIV infection." Immunological Reviews 159, no. 1 (October 1997): 49–67. http://dx.doi.org/10.1111/j.1600-065x.1997.tb01006.x.

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14

Popik, Waldemar, Timothy M. Alce, and Wei-Chun Au. "Human Immunodeficiency Virus Type 1 Uses Lipid Raft-Colocalized CD4 and Chemokine Receptors for Productive Entry into CD4+ T Cells." Journal of Virology 76, no. 10 (May 15, 2002): 4709–22. http://dx.doi.org/10.1128/jvi.76.10.4709-4722.2002.

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ABSTRACT In this report, we describe a crucial role of lipid raft-colocalized receptors in the entry of human immunodeficiency virus type 1 (HIV-1) into CD4+ T cells. We show that biochemically isolated detergent-resistant fractions have characteristics of lipid rafts. Lipid raft integrity was required for productive HIV-1 entry as determined by (i) semiquantitative PCR analysis and (ii) single-cycle infectivity assay using HIV-1 expressing the luciferase reporter gene and pseudotyped with HIV-1 HXB2 envelope or vesicular stomatitis virus envelope glycoprotein (VSV-G). Depletion of plasma membrane cholesterol with methyl-β-cyclodextrin (MβCD) relocalized raft-resident markers to a nonraft environment but did not significantly change the surface expression of HIV-1 receptors. MβCD treatment inhibited productive infection of HIV-1 by 95% as determined by luciferase activity in cells infected with HXB2 envelope-pseudotyped virus. In contrast, infection with VSV-G-pseudotyped virus, which enters the cells through an endocytic pathway, was not suppressed. Biochemical fractionation and confocal imaging of HIV-1 receptor distribution in live cells demonstrated that CD4, CCR5, and CXCR4 colocalized with raft-resident markers, ganglioside GM1, and glycosylphosphatidylinositol-anchored CD48. While confocal microscopy analysis revealed that HIV-1 receptors localized most likely to the same lipid microdomains, sucrose gradient analysis of the receptor localization showed that, in contrast to CD4 and CCR5, CXCR4 was associated preferentially with the nonraft membrane fraction. The binding of HIV-1 envelope gp120 to lipid rafts in the presence, but not in the absence, of cholesterol strongly supports our hypothesis that raft-colocalized receptors are directly involved in virus entry. Dramatic changes in lipid raft and HIV-1 receptor redistribution were observed upon binding of HIV-1 NL4-3 to PM1 T cells. Colocalization of CCR5 with GM1 and gp120 upon engagement of CD4 and CXCR4 by HIV-1 further supports our observation that HIV-1 receptors localize to the same lipid rafts in PM1 T cells.

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15

Terra Junior, Orlando, Guilherme Alfradique, Gabriel Maldonado, and Adriano Arnobio. "A cross-sectional study of C-type lectin receptors (CD94 and CD314) in patients with HIV/AIDS and cancer." Global Perspectives on Medical Sciences 1, no. 1 (July 18, 2017): 003. http://dx.doi.org/10.26535/gpms.v1i1.7.

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The HIV-1 induces functional and phenotypic changes in the activation profile of NK cells. The cancers arising from immunosuppression induce an increase of pro-inflammatory cytokines in the tumor microenvironment, which can result in altered expression of these receptors in lymphocyte subpopulations, including T lymphocytes, NK cells and NKT cells. In the current study, we investigated possible HIV/AIDS-related changes in the expression of the C-type lectin receptors comparing healthy donors, HIV/AIDS patients, and HIV/AIDS patients with cancer (HIV/AIDSWC). The expression of these receptors was examined in the total NK cell population and CD56dim and CD56bright NK cell subsets separately and T- and NKT-cell populations. There was a significant increase of the expression of NKG2D (CD134) in T lymphocytes in HIV/AIDS and HIV/AIDSWC compared to healthy donors. There were no significant changes of this receptor in NK cells (and their subtypes) and NKT to compare them with healthy donors. As for the CD94 receptor, there were no significant changes of this receptor on NK cells (and their subtypes), NKT cells and T Lymphocyte to compare them with healthy donors, except for the increase in percentage of the expression in CD56bright cells, however this was not true in absolute terms.

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16

Bracci, Luisa, Samir K. Ballas, Adriano Spreafico, and Paolo Neri. "Molecular Mimicry Between the Rabies Virus Glycoprotein and Human Immunodeficiency Virus-1 GP120: Cross-Reacting Antibodies Induced by Rabies Vaccination." Blood 90, no. 9 (November 1, 1997): 3623–28. http://dx.doi.org/10.1182/blood.v90.9.3623.

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Abstract The 160-170 sequence of human immunodeficiency virus (HIV)-1 gp120 mimics a nicotinic receptor-binding motif of rabies virus glycoprotein and snake neurotoxins. This sequence has been proposed to be involved in the binding of HIV-1 gp120 to the acetylcholine binding sites of nicotinic receptors. By using biomolecular interaction analysis (BIA) technology we have found that HIV-1 gp120 can bind to detergent-extracted nicotinic receptor from fetal calf muscle. The binding is inhibited by nicotine and by a synthetic peptide reproducing the gp120 160-170 sequence. The molecular mimicry between gp120 and rabies virus glycoprotein is confirmed by cross-reacting antibodies. We have found that vaccination against rabies can induce the production of anti–HIV-1 gp120 antibodies in humans. The cross-reacting antibodies are directed to the gp120 sequence involved in the mimicry with the rabies virus glycoprotein. The cross-reactivity between the rabies virus and HIV-1 has important implications in transfusion medicine. Moreover, the presence of cross-reacting antibodies between the nicotinic receptor binding site of rabies virus glycoprotein and a fragment of HIV-1 gp120 strengthens the hypothesis about the possible role of nicotinic receptors as potential receptors for HIV-1 in the central nervous system.

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17

Snyder, Greg A., Jennifer Ford, Parizad Torabi-Parizi, James A. Arthos, Peter Schuck, Marco Colonna, and Peter D. Sun. "Characterization of DC-SIGN/R Interaction with Human Immunodeficiency Virus Type 1 gp120 and ICAM Molecules Favors the Receptor's Role as an Antigen-Capturing Rather than an Adhesion Receptor." Journal of Virology 79, no. 8 (April 15, 2005): 4589–98. http://dx.doi.org/10.1128/jvi.79.8.4589-4598.2005.

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ABSTRACT The dendritic cell (DC)-specific intercellular adhesion molecule 3 (ICAM-3)-grabbing nonintegrin binding receptor (DC-SIGN) was shown to bind human immunodeficiency virus type 1 (HIV-1) viral envelope protein gp120 and proposed to function as a Trojan horse to enhance trans-virus infection to host T cells. To better understand the mechanism by which DC-SIGN and DC-SIGNR selectively bind HIV-1 gp120, we constructed a series of deletion mutations in the repeat regions of both receptors. Different truncated receptors exist in different oligomeric forms. The carbohydrate binding domain without any repeats was monomeric, whereas the full extracellular receptors existed as tetramers. All reconstituted receptors retained their ability to bind gp120. The dissociation constant, however, differed drastically from micromolar values for the monomeric receptors to nanomolar values for the tetrameric receptors, suggesting that the repeat region of these receptors contributes to the avidity of gp120 binding. Such oligomerization may provide a mechanism for the receptor to selectively recognize pathogens containing multiple high-mannose-concentration carbohydrates. In contrast, the receptors bound to ICAMs with submicromolar affinities that are similar to those of two nonspecific cell surface glycoproteins, FcγRIIb and FcγRIII, and the oligomerization of DC-SIGNR resulted in no increase in binding affinity to ICAM-3. These findings suggest that DC-SIGN may not discriminate other cell surface glycoproteins from ICAM-3 binding. The pH dependence in DC-SIGN binding to gp120 showed that the receptor retained high-affinity gp120 binding at neutral pH but lost gp120 binding at pH 5, suggesting a release mechanism of HIV in the acidic endosomal compartment by DC-SIGN. Our work contradicts the function of DC-SIGN as a Trojan horse to facilitate HIV-1 infection; rather, it supports the function of DC-SIGN/R (a designation referring to both DC-SIGN and DC-SIGNR) as an antigen-capturing receptor.

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18

Rivera-Morales, Lydia Guadalupe, Paulo Lopez-Guillen, Jose Manuel Vazquez-Guillen, Gerardo C. Palacios-Saucedo, Adrian G. Rosas-Taraco, Antonio Ramirez-Pineda, Patricia Irene Amaya-Garcia, and Cristina Rodriguez-Padilla. "Expression of CCR5, CXCR4 and DC-SIGN in Cervix of HIV-1 Heterosexually Infected Mexican Women." Open AIDS Journal 6, no. 1 (October 5, 2012): 239–44. http://dx.doi.org/10.2174/1874613601206010239.

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Background:A number of studies have demonstrated that receptor and co-receptor expression levels which may affect viral entry, promoting cervical HIV infection. The aim was to evaluate the expression levels of CCR5, CXCR4and DC-SIGN mRNA in a sample of heterosexually HIV infected Mexican women.Methods:We enrolled twenty-six HIV heterosexual infected women attending a local infectious diseases medical unit.RNA was isolated from the cervix and gene expression analysis was performed using real-time PCR.Results:Expression rates for mRNA of CCR5 (median 1.82; range 0.003–2934) were higher than those observed for CXCR4 (0.79; 0.0061–3312) and DC-SIGN (0.33; 0.006–532) receptors (p < 0.05). A high correlation was found between the mRNA expression levels of these three receptors (rs = 0.52 to 0.85, p < 0.01).Conclusion:Levels of expression of the tested chemokine receptors in the cervix are different from each other and alsovary from woman to woman, and seem to support the suggestion that chemokine receptor expression in genital tissues may be playing a role in the HIV transmission.

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Grande, Fedora, Maria Occhiuzzi, Bruno Rizzuti, Giuseppina Ioele, Michele De Luca, Paola Tucci, Valentina Svicher, Stefano Aquaro, and Antonio Garofalo. "CCR5/CXCR4 Dual Antagonism for the Improvement of HIV Infection Therapy." Molecules 24, no. 3 (February 2, 2019): 550. http://dx.doi.org/10.3390/molecules24030550.

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HIV entry in the host cell requires the interaction with the CD4 membrane receptor, and depends on the activation of one or both co-receptors CCR5 and CXCR4. Former selective co-receptor antagonists, acting at early stages of infection, are able to impair the receptor functions, preventing the viral spread toward AIDS. Due to the capability of HIV to develop resistance by switching from CCR5 to CXCR4, dual co-receptor antagonists could represent the next generation of AIDS prophylaxis drugs. We herein present a survey on relevant results published in the last few years on compounds acting simultaneously on both co-receptors, potentially useful as preventing agents or in combination with classical anti-retroviral drugs based therapy.

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20

Moore, John P., Alexandra Trkola, and Tatjana Dragic. "Co-receptors for HIV-1 entry." Current Opinion in Immunology 9, no. 4 (August 1997): 551–62. http://dx.doi.org/10.1016/s0952-7915(97)80110-0.

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21

Sanders, Virginia J., Christopher A. Pittman, Michael G. White, Guoji Wang, Clayton A. Wiley, and Cristian L. Achim. "Chemokines and receptors in HIV encephalitis." AIDS 12, no. 9 (September 1998): 1021–26. http://dx.doi.org/10.1097/00002030-199809000-00009.

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22

D'Souza, M. Patricia, and Victoria Harden. "Chemokines and HIV–1 second receptors." Nature Medicine 2, no. 12 (December 1996): 1293–300. http://dx.doi.org/10.1038/nm1296-1293.

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23

Clapham, Paul R., and Áine McKnight. "HIV-1 receptors and cell tropism." British Medical Bulletin 58, no. 1 (September 1, 2001): 43–59. http://dx.doi.org/10.1093/bmb/58.1.43.

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Bristow, Cynthia L., Danielle R. Mercatante, and Ryszard Kole. "HIV-1 preferentially binds receptors copatched with cell-surface elastase." Blood 102, no. 13 (December 15, 2003): 4479–86. http://dx.doi.org/10.1182/blood-2003-05-1635.

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Abstract Human leukocyte elastase (HLE) interacts with HIV-1 glycoprotein (gp)41, suggesting a nonenzymatic receptor function for HLE in the context of HIV-1. HLE is found localized to the cell surface, but not granules in HIV permissive clones, and to granules, but not the cell surface of HIV nonpermissive clones. Inducing cell-surface HLE expression on HLE null, HIV nonpermissive clones permits HIV infectivity. HIV binding and infectivity diminish in proportion to HLE RNA subtraction. HIV binding and infectivity show dose dependence for the natural HLE ligand α1 proteinase inhibitor (α1antitrypsin, α1PI). Chemokines prevent, whereas α1PI promotes, copatching of HLE with the canonical HIV receptors. Recent demonstration that decreased viral RNA is significantly correlated with decreased circulating α1PI in HIV seropositive individuals is consistent with a model in which HLE and α1PI can serve as HIV coreceptor and cofactor, respectively, and potentially participate in the pathophysiology of HIV disease progression. (Blood. 2003;102:4479-4486)

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Shen, Hongmei, Tao Cheng, Frederick I. Preffer, David Dombkowski, Michael H. Tomasson, David E. Golan, Otto Yang, et al. "Intrinsic Human Immunodeficiency Virus Type 1 Resistance of Hematopoietic Stem Cells Despite Coreceptor Expression." Journal of Virology 73, no. 1 (January 1, 1999): 728–37. http://dx.doi.org/10.1128/jvi.73.1.728-737.1999.

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ABSTRACT Interactions of human immunodeficiency virus type 1 (HIV-1) with hematopoietic stem cells may define restrictions on immune reconstitution following effective antiretroviral therapy and affect stem cell gene therapy strategies for AIDS. In the present study, we demonstrated mRNA and cell surface expression of HIV-1 receptors CD4 and the chemokine receptors CCR-5 and CXCR-4 in fractionated cells representing multiple stages of hematopoietic development. Chemokine receptor function was documented in subsets of cells by calcium flux in response to a cognate ligand. Productive infection by HIV-1 via these receptors was observed with the notable exception of stem cells, in which case the presence of CD4, CXCR-4, and CCR-5, as documented by single-cell analysis for expression and function, was insufficient for infection. Neither productive infection, transgene expression, nor virus entry was detectable following exposure of stem cells to either wild-type HIV-1 or lentivirus constructs pseudotyped in HIV-1 envelopes of macrophage-tropic, T-cell-tropic, or dualtropic specificity. Successful entry into stem cells of a vesicular stomatitis virus G protein-pseudotyped HIV-1 construct demonstrated that the resistance to HIV-1 was mediated at the level of virus-cell membrane fusion and entry. These data define the hematopoietic stem cell as a sanctuary cell which is resistant to HIV-1 infection by a mechanism independent of receptor and coreceptor expression that suggests a novel means of cellular protection from HIV-1.

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Meyerson, Nicholas R., Amit Sharma, Gregory K. Wilkerson, Julie Overbaugh, and Sara L. Sawyer. "Identification of Owl Monkey CD4 Receptors Broadly Compatible with Early-Stage HIV-1 Isolates." Journal of Virology 89, no. 16 (June 10, 2015): 8611–22. http://dx.doi.org/10.1128/jvi.00890-15.

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ABSTRACTMost HIV-1 variants isolated from early-stage human infections do not use nonhuman primate versions of the CD4 receptor for cellular entry, or they do so poorly. We and others have previously shown thatCD4has experienced strong natural selection over the course of primate speciation, but it is unclear whether this selection has influenced the functional characteristics of CD4 as an HIV-1 receptor. Surprisingly, we find that selection onCD4has been most intense in the New World monkeys, animals that have never been found to harbor lentiviruses related to HIV-1. Based on this, we sampledCD4genetic diversity within populations of individuals from seven different species, including five species of New World monkeys. We found that some, but not all,CD4alleles found in Spix's owl monkeys (Aotus vociferans) encode functional receptors for early-stage human HIV-1 isolates representing all of the major group M clades (A, B, C, and D). However, only some isolates of HIV-1 subtype C can use the CD4 receptor encoded by permissive Spix's owl monkey alleles. We characterized the prevalence of functionalCD4alleles in a colony of captive Spix's owl monkeys and found that 88% of surveyed individuals are homozygous for permissiveCD4alleles, which encode an asparagine at position 39 of the receptor. We found that the CD4 receptors encoded by two other species of owl monkeys (Aotus azarae andAotus nancymaae) also serve as functional entry receptors for early-stage isolates of HIV-1.IMPORTANCENonhuman primates, particularly macaques, are used for preclinical evaluation of HIV-1 vaccine candidates. However, a significant limitation of the macaque model is the fact that most circulating HIV-1 variants cannot use the macaque CD4 receptor to enter cells and have to be adapted to these species. This is particularly true for viral variants from early stages of infection, which represent the most relevant vaccine targets. In this study, we found that some individuals from captive owl monkey populations harborCD4alleles that are compatible with a broad collection of HIV-1 isolates, including those isolated from early in infection in highly affected populations and representing diverse subtypes.

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Owman, Christer, Alfredo Garzino-Demo, Fiorenza Cocchi, Mikulas Popovic, Alan Sabirsh, and Robert C. Gallo. "The leukotriene B4receptor functions as a novel type of coreceptor mediating entry of primary HIV-1 isolates into CD4-positive cells." Proceedings of the National Academy of Sciences 95, no. 16 (August 4, 1998): 9530–34. http://dx.doi.org/10.1073/pnas.95.16.9530.

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The recently cloned human chemoattractant receptor-like (CMKRL)1, which is expressedin vivoin CD4-positive immune cells, has structural homology with the two chemokine receptors C-C chemokine receptor (CCR)5 and C-X-C chemokine receptor (CXCR)4, which serve as the major coreceptors necessary for fusion of the HIV-1 envelope with target cells. In view of the structural similarity, CMKRL1 was tested for its possible function as another HIV-1 coreceptor after stable expression in murine fibroblasts bearing the human CD4 receptor. The cells were infected with 10 primary clinical isolates of HIV-1, and entry was monitored by semiquantitative PCR of viral DNA. The efficiency of the entry was compared with the entry taking place in CD4-positive cells expressing either CCR5 or CXCR4. Seven of the isolates used CMKRL1 for viral entry; they were mainly of the syncytium-inducing phenotype and also used CXCR4. Entry efficiency was higher with CMKRL1 than with CXCR4 for more than half of these isolates. Three of the ten isolates did not use CMKRL1; instead, entry was mediated by both CCR5 and CXCR4. The experiments thus indicate that CMKRL1 functions as a coreceptor for the entry of HIV-1 into CD4-positive cells. In the course of this study, leukotriene B4was shown to be the natural ligand for this receptor (now designated BLTR), which therefore represents a novel type of HIV-1 coreceptor along with the previously identified chemokine receptors. BLTR belongs to the same general chemoattractant receptor family as the chemokine receptors but is structurally more distant from them than are any of the previously described HIV-1 coreceptors.

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SCHEIDEGGER, Patrick, Wolfgang WEIGLHOFER, Stéphanie SUAREZ, Sandra CONSOLE, Johannes WALTENBERGER, Michael S. PEPPER, Rolf JAUSSI, and Kurt BALLMER-HOFER. "Signalling properties of an HIV-encoded angiogenic peptide mimicking vascular endothelial growth factor activity." Biochemical Journal 353, no. 3 (January 25, 2001): 569–78. http://dx.doi.org/10.1042/bj3530569.

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HIV-1 expresses a multifunctional protein called TAT (trans-acting transcriptional activator), the function of which in vivo is tightly correlated with the incidence of Kaposi's sarcoma in AIDS patients. TAT is angiogenic and apparently binds to receptors specific for vascular endothelial growth factor (VEGF). Amino acids 46–60 of HIV-TAT, known as the basic peptide, have been shown to be responsible for its functional interaction with VEGF receptors. To characterize further the binding properties of this peptide, its coding sequence was fused to the reading frame of bacterial thioredoxin, allowing the production of large amounts of chimaeric polypeptides in bacteria in a biologically active form. Binding of chimaeric proteins to VEGF receptors was studied in vitro in endothelial cell cultures expressing either of the two receptors. Chimaeric thioredoxin proteins carrying the basic domain of TAT bound to both VEGF receptors with affinities similar to those of HIV-TAT or VEGF. Interestingly, these polypeptides competed only partially with VEGF for receptor binding, implying different binding sites for the TAT peptide and VEGF. This suggests that TAT binds VEGF receptors at new sites that might be useful targets for pharmacological intervention during pathological angiogenesis. The thioredoxin/basic-peptide chimaeras are functional agonists that mediate VEGF receptor signalling: (1) they stimulate the growth of endothelial cells; (2) together with basic fibroblast growth factor they cause tube formation of endothelial cells in collagen gels; (3) they induce blood vessel formation on the chicken chorioallantoic membrane; and (4) they activate VEGF receptor kinase and mitogen-activated protein kinase activity.

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Liao, Fang, Ghalib Alkhatib, Keith W. C. Peden, Geetika Sharma, Edward A. Berger, and Joshua M. Farber. "STRL33, A Novel Chemokine Receptor–like Protein, Functions as a Fusion Cofactor for Both Macrophage-tropic and T Cell Line–tropic HIV-1." Journal of Experimental Medicine 185, no. 11 (June 2, 1997): 2015–23. http://dx.doi.org/10.1084/jem.185.11.2015.

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The chemokine receptors CXCR4, CCR2B, CCR3, and CCR5 have recently been shown to serve along with CD4 as coreceptors for HIV-1. The tropisms of HIV-1 strains for subgroups of CD4+ cells can be explained, at least partly, by the selective use of G protein–coupled receptors (GPCRs). We have identified a novel human gene, STRL33, located on chromosome 3 that encodes a GPCR with sequence similarity to chemokine receptors and to chemokine receptor–like orphan receptors. STRL33 is expressed in lymphoid tissues and activated T cells, and is induced in activated peripheral blood lymphocytes. When transfected into nonhuman NIH 3T3 cells expressing human CD4, the STRL33 cDNA rendered these cells competent to fuse with cells expressing HIV-1 envelope glycoproteins (Envs). Of greatest interest, STRL33, in contrast with CXCR4 or CCR5, was able to function as a cofactor for fusion mediated by Envs from both T cell line–tropic and macrophage-tropic HIV-1 strains. STRL33-transfected Jurkat cell lines also supported enhanced productive infection with HIV-1 compared with control Jurkat cells. Despite the sequence similarities between STRL33 and chemokine receptors, STRL33-transfected cell lines did not respond to any in a panel of chemokines. Based on the pattern of tissue expression of the STRL33 mRNA, and given the ability of STRL33 to function with Envs of differing tropisms, STRL33 may play a role in the establishment and/or progression of HIV-1 infection.

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Ghorpade, Anuja, Meng Qi Xia, Bradley T. Hyman, Yuri Persidsky, Adeline Nukuna, Paul Bock, Myhanh Che, Jenae Limoges, Howard E. Gendelman, and Charles R. Mackay. "Role of the β-Chemokine Receptors CCR3 and CCR5 in Human Immunodeficiency Virus Type 1 Infection of Monocytes and Microglia." Journal of Virology 72, no. 4 (April 1, 1998): 3351–61. http://dx.doi.org/10.1128/jvi.72.4.3351-3361.1998.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) infection in mononuclear phagocyte lineage cells (monocytes, macrophages, and microglia) is a critical component in the pathogenesis of viral infection. Viral replication in macrophages serves as a reservoir, a site of dissemination, and an instigator for neurological sequelae during HIV-1 disease. Recent studies demonstrated that chemokine receptors are necessary coreceptors for HIV-1 entry which determine viral tropism for different cell types. To investigate the relative contribution of the β-chemokine receptors CCR3 and CCR5 to viral infection of mononuclear phagocytes we utilized a panel of macrophage-tropic HIV-1 strains (from blood and brain tissue) to infect highly purified populations of monocytes and microglia. Antibodies to CD4 (OKT4A) abrogated HIV-1 infection. The β chemokines and antibodies to CCR3 failed to affect viral infection of both macrophage cell types. Antibodies to CCR5 (3A9) prevented monocyte infection but only slowed HIV replication in microglia. Thus, CCR5, not CCR3, is an essential receptor for HIV-1 infection of monocytes. Microglia express both CCR5 and CCR3, but antibodies to them fail to inhibit viral entry, suggesting the presence of other chemokine receptors for infection of these cells. These studies demonstrate the importance of mononuclear phagocyte heterogeneity in establishing HIV-1 infection and persistence.

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Shen, Ruizhong, Holly E. Richter, Ronald H. Clements, Lea Novak, Kayci Huff, Diane Bimczok, Sumathi Sankaran-Walters, et al. "Macrophages in Vaginal but Not Intestinal Mucosa Are Monocyte-Like and Permissive to Human Immunodeficiency Virus Type 1 Infection." Journal of Virology 83, no. 7 (January 19, 2009): 3258–67. http://dx.doi.org/10.1128/jvi.01796-08.

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ABSTRACT Mucosal surfaces play a major role in human immunodeficiency virus type 1 (HIV-1) transmission and pathogenesis, and yet the role of lamina propria macrophages in mucosal HIV-1 infection has received little investigative attention. We report here that vaginal and intestinal macrophages display distinct phenotype and HIV-1 permissiveness profiles. Vaginal macrophages expressed the innate response receptors CD14, CD89, CD16, CD32, and CD64 and the HIV-1 receptor/coreceptors CD4, CCR5, and CXCR4, similar to monocytes. Consistent with this phenotype, green fluorescent protein-tagged R5 HIV-1 entered macrophages in explanted vaginal mucosa as early as 30 min after inoculation of virus onto the epithelium, and purified vaginal macrophages supported substantial levels of HIV-1 replication by a panel of highly macrophage-tropic R5 viruses. In sharp contrast, intestinal macrophages expressed no detectable, or very low levels of, innate response receptors and HIV-1 receptor/coreceptors and did not support HIV-1 replication, although virus occasionally entered macrophages in intestinal tissue explants. Thus, vaginal, but not intestinal, macrophages are monocyte-like and permissive to R5 HIV-1 after the virus has translocated across the epithelium. These findings suggest that genital and gut macrophages have different roles in mucosal HIV-1 pathogenesis and that vaginal macrophages play a previously underappreciated but potentially important role in mucosal HIV-1 infection in the female genital tract.

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Moir, Susan, Jason Ho, Angela Malaspina, Wei Wang, Angela C. DiPoto, Marie A. O'Shea, Gregg Roby, et al. "Evidence for HIV-associated B cell exhaustion in a dysfunctional memory B cell compartment in HIV-infected viremic individuals." Journal of Experimental Medicine 205, no. 8 (July 14, 2008): 1797–805. http://dx.doi.org/10.1084/jem.20072683.

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Human immunodeficiency virus (HIV) disease leads to impaired B cell and antibody responses through mechanisms that remain poorly defined. A unique memory B cell subpopulation (CD20hi/CD27lo/CD21lo) in human tonsillar tissues was recently defined by the expression of the inhibitory receptor Fc-receptor-like-4 (FCRL4). In this study, we describe a similar B cell subpopulation in the blood of HIV-viremic individuals. FCRL4 expression was increased on B cells of HIV-viremic compared with HIV-aviremic and HIV-negative individuals. It was enriched on B cells with a tissuelike memory phenotype (CD20hi/CD27−/CD21lo) when compared with B cells with a classical memory (CD27+) or naive (CD27−/CD21hi) B cell phenotype. Tissuelike memory B cells expressed patterns of homing and inhibitory receptors similar to those described for antigen-specific T cell exhaustion. The tissuelike memory B cells proliferated poorly in response to B cell stimuli, which is consistent with high-level expression of multiple inhibitory receptors. Immunoglobulin diversities and replication histories were lower in tissuelike, compared with classical, memory B cells, which is consistent with premature exhaustion. Strikingly, HIV-specific responses were enriched in these exhausted tissuelike memory B cells, whereas total immunoglobulin and influenza-specific responses were enriched in classical memory B cells. These data suggest that HIV-associated premature exhaustion of B cells may contribute to poor antibody responses against HIV in infected individuals.

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Owen, Sherry M., Dennis Ellenberger, Mark Rayfield, Stefan Wiktor, Philippe Michel, Michael H. Grieco, Feng Gao, Beatrice H. Hahn, and Renu B. Lal. "Genetically Divergent Strains of Human Immunodeficiency Virus Type 2 Use Multiple Coreceptors for Viral Entry." Journal of Virology 72, no. 7 (July 1, 1998): 5425–32. http://dx.doi.org/10.1128/jvi.72.7.5425-5432.1998.

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ABSTRACT Several members of the seven-transmembrane chemokine receptor family have been shown to serve, with CD4, as coreceptors for entry by human immunodeficiency virus type 1 (HIV-1). While coreceptor usage by HIV-1 primary isolates has been studied by several groups, there is only limited information available concerning coreceptor usage by primary HIV-2 isolates. In this study, we have analyzed coreceptor usage of 15 primary HIV-2 isolates, using lymphocytes from a donor with nonfunctional CCR5 (CCR5 −/−; homozygous 32-bp deletion). Based on the infections of PBMCs, seven of these primary isolates had an absolute requirement for CCR5 expression, whereas the remaining eight exhibited a broader coreceptor usage. All CCR5-requiring isolates were non-syncytium inducing, whereas isolates utilizing multiple coreceptors were syncytium inducing. Blocking experiments using known ligands for chemokine receptors provided indirect evidence for additional coreceptor utilization by primary HIV-2 isolates. Analysis of GHOST4 cell lines expressing various chemokine receptors (CCR1, CCR2b, CCR3, CCR4, CCR5, CXCR4, BONZO, and BOB) further defined specific coreceptor usage of primary HIV-2 isolates. The receptors used included CXCR4, CCR1-5, and the recently described receptors BONZO and BOB. However, the efficiency at which the coreceptors were utilized varied greatly among the various isolates. Analysis of V3 envelope sequences revealed no specific motif that correlated with coreceptor usage. Our data demonstrate that primary HIV-2 isolates are capable of using a broad range of coreceptors for productive infection in vitro. Additionally, our data suggest that expanded coreceptor usage by HIV-2 may correlate with disease progression.

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Lee, Benhur, Benjamin J. Doranz, Shalini Rana, Yanji Yi, Mario Mellado, Jose M. R. Frade, Carlos Martinez-A., et al. "Influence of the CCR2-V64I Polymorphism on Human Immunodeficiency Virus Type 1 Coreceptor Activity and on Chemokine Receptor Function of CCR2b, CCR3, CCR5, and CXCR4." Journal of Virology 72, no. 9 (September 1, 1998): 7450–58. http://dx.doi.org/10.1128/jvi.72.9.7450-7458.1998.

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ABSTRACT The chemokine receptors CCR5 and CXCR4 are used by human immunodeficiency virus type 1 (HIV-1) in conjunction with CD4 to infect cells. In addition, some virus strains can use alternative chemokine receptors, including CCR2b and CCR3, for infection. A polymorphism inCCR2 (CCR2-V64I) is associated with a 2- to 4-year delay in the progression to AIDS. To investigate the mechanism of this protective effect, we studied the expression of CCR2b and CCR2b-V64I, their chemokine and HIV-1 coreceptor activities, and their effects on the expression and receptor activities of the major HIV-1 coreceptors. CCR2b and CCR2b-V64I were expressed at similar levels, and neither molecule affected the expression or coreceptor activity of CCR3, CCR5, or CXCR4 in cotransfected cell lines. Peripheral blood mononuclear cells (PBMCs) from CCR2-V64I heterozygotes had normal levels of CCR2b and CCR5 but slightly reduced levels of CXCR4. CCR2b and CCR2b-V64I functioned equally well as HIV-1 coreceptors, and CCR2-V64I PBMCs were permissive for HIV-1 infection regardless of viral tropism. The MCP-1-induced calcium mobilization mediated by CCR2b signaling was unaffected by the polymorphism, but MCP-1 signaling mediated by either CCR2b- or CCR2-V64I-encoded receptors resulted in heterologous desensitization (i.e., limiting the signal response of other receptors) of both CCR5 and CXCR4. The heterologous desensitization of CCR5 and CXCR4 signaling by bothCCR2 allele receptor types provides a mechanistic link that might help explain the in vivo effects of CCR2 gene variants on progression to AIDS as well as the reported antiviral activity of natural CCR2 ligands.

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Pett, SL, S. Emery, AD Kelleher, and DA Cooper. "Antiretroviral agents: Focus on Maraviroc for the Treatment of HIV-1-Infected Adults." Clinical Medicine Insights: Therapeutics 2 (January 2010): CMT.S5420. http://dx.doi.org/10.4137/cmt.s5420.

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Over a decade has passed since several groups identified the chemokine receptors CXCR4 and CCR5 as key co-receptors for HIV entry. CCR5 is more important in HIV transmission and during the early course of HIV infection. It is also apparent that protection from HIV infection is afforded to those lacking CCR5–-the so called delta-32 homozygotes; in those heterozygous for this mutation, an attenuated course of HIV-infection is observed. Provocatively, those with modified expression of CCR5 are physiologically normal with the exception of poorer outcomes with some of the viral encephalitides specifically West Nile virus and Tick Borne encephalitis. The small molecule, orally-bioavailable CCR5 receptor antagonists, including, maraviroc (MVC), are allosteric inhibitors that lock the CCR5 receptor into a conformation such that the receptor is not able to bind HIV envelope protein; the molecules also variably block intracellular signalling induced by different receptor-binding chemokines. The aims of this review on the CCR5 receptor inhibitors are to summarise information relevant to treatment in individuals with HIV-1 infection. Data from the licensing studies, the side-effect profile and putative long-term risks of CCR5 receptor inhibitor exposure, tropism testing and mechanisms of resistance will be reviewed. The potential for using this class of agent as an immunomodulating agent will be detailed. Given that MVC is the only licensed drug in this class at present and reflecting the greater body of work describing this agent, the majority of information in this review relates to MVC. Last, the authors propose the place of MVC in the hierarchy of HIV therapy and future opportunities for research.

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O’Connell, Amalfitano, and Aldhamen. "SLAM Family Receptor Signaling in Viral Infections: HIV and Beyond." Vaccines 7, no. 4 (November 16, 2019): 184. http://dx.doi.org/10.3390/vaccines7040184.

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The signaling lymphocytic activation molecule (SLAM) family of receptors are expressed on the majority of immune cells. These receptors often serve as self-ligands, and play important roles in cellular communication and adhesion, thus modulating immune responses. SLAM family receptor signaling is differentially regulated in various immune cell types, with responses generally being determined by the presence or absence of two SLAM family adaptor proteins—Ewing’s sarcoma-associated transcript 2 (EAT-2) and SLAM-associated adaptor protein (SAP). In addition to serving as direct regulators of the immune system, certain SLAM family members have also been identified as direct targets for specific microbes and viruses. Here, we will discuss the known roles for these receptors in the setting of viral infection, with special emphasis placed on HIV infection. Because HIV causes such complex dysregulation of the immune system, studies of the roles for SLAM family receptors in this context are particularly exciting.

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McKnight, Áine, Matthias T. Dittmar, José Moniz-Periera, Koya Ariyoshi, Jacqueline D. Reeves, Sam Hibbitts, Denise Whitby, et al. "A Broad Range of Chemokine Receptors Are Used by Primary Isolates of Human Immunodeficiency Virus Type 2 as Coreceptors with CD4." Journal of Virology 72, no. 5 (May 1, 1998): 4065–71. http://dx.doi.org/10.1128/jvi.72.5.4065-4071.1998.

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ABSTRACT Like human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV), HIV-2 requires a coreceptor in addition to CD4 for entry into cells. HIV and SIV coreceptor molecules belong to a family of seven-transmembrane-domain G-protein-coupled receptors. Here we show that primary HIV-2 isolates can use a broad range of coreceptor molecules, including CCR1, CCR2b, CCR3, CCR4, CCR5, and CXCR4. Despite broad coreceptor use, the chemokine ligand SDF-1 substantially blocked HIV-2 infectivity of peripheral blood mononuclear cells, indicating that its receptor, CXCR4, was the predominant coreceptor for infection of these cells. However, expression of CXCR4 together with CD4 on some cell types did not confer susceptibility to infection by all CXCR4-using virus isolates. These data therefore indicate that another factor(s) influences the ability of HIV-2 to replicate in human cell types that express the appropriate receptors for virus entry.

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Reeves, Jacqueline D., Sam Hibbitts, Graham Simmons, Áine McKnight, José M. Azevedo-Pereira, José Moniz-Pereira, and Paul R. Clapham. "Primary Human Immunodeficiency Virus Type 2 (HIV-2) Isolates Infect CD4-Negative Cells via CCR5 and CXCR4: Comparison with HIV-1 and Simian Immunodeficiency Virus and Relevance to Cell Tropism In Vivo." Journal of Virology 73, no. 9 (September 1, 1999): 7795–804. http://dx.doi.org/10.1128/jvi.73.9.7795-7804.1999.

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ABSTRACT Cell surface receptors exploited by human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) for infection are major determinants of tropism. HIV-1 usually requires two receptors to infect cells. Gp120 on HIV-1 virions binds CD4 on the cell surface, triggering conformational rearrangements that create or expose a binding site for a seven-transmembrane (7TM) coreceptor. Although HIV-2 and SIV strains also use CD4, several laboratory-adapted HIV-2 strains infect cells without CD4, via an interaction with the coreceptor CXCR4. Moreover, the envelope glycoproteins of SIV of macaques (SIVMAC) can bind to and initiate infection of CD4− cells via CCR5. Here, we show that most primary HIV-2 isolates can infect either CCR5+ or CXCR4+ cells without CD4. The efficiency of CD4-independent infection by HIV-2 was comparable to that of SIV, but markedly higher than that of HIV-1. CD4-independent HIV-2 strains that could use both CCR5 and CXCR4 to infect CD4+cells were only able to use one of these receptors in the absence of CD4. Our observations therefore indicate (i) that HIV-2 and SIV envelope glycoproteins form a distinct conformation that enables contact with a 7TM receptor without CD4, and (ii) the use of CD4 enables a wider range of 7TM receptors to be exploited for infection and may assist adaptation or switching to new coreceptors in vivo. Primary CD4− fetal astrocyte cultures expressed CXCR4 and supported replication by the T-cell-line-adapted ROD/B strain. Productive infection by primary X4 strains was only triggered upon treatment of virus with soluble CD4. Thus, many primary HIV-2 strains infect CCR5+ or CXCR4+ cell lines without CD4 in vitro. CD4− cells that express these coreceptors in vivo, however, may still resist HIV-2 entry due to insufficient coreceptor concentration on the cell surface to trigger fusion or their expression in a conformation nonfunctional as a coreceptor. Our study, however, emphasizes that primary HIV-2 strains carry the potential to infect CD4− cells expressing CCR5 or CXCR4 in vivo.

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Qureshi, Amer, Richard Zheng, Terry Parlett, Xiaoju Shi, Priyadhashini Balaraman, Sihem Cheloufi, Brendan Murphy, Christine Guntermann, and Peter Eagles. "Gene silencing of HIV chemokine receptors using ribozymes and single-stranded antisense RNA." Biochemical Journal 394, no. 2 (February 10, 2006): 511–18. http://dx.doi.org/10.1042/bj20051268.

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The chemokine receptors CXCR4 and CCR5 are required for HIV-1 to enter cells, and the progression of HIV-1 infection to AIDS involves a switch in the co-receptor usage of the virus from CCR5 to CXCR4. These receptors therefore make attractive candidates for therapeutic intervention, and we have investigated the silencing of their genes by using ribozymes and single-stranded antisense RNAs. In the present study, we demonstrate using ribozymes that a depletion of CXCR4 and CCR5 mRNAs can be achieved simultaneously in human PBMCs (peripheral blood mononuclear cells), cells commonly used by the virus for infection and replication. Ribozyme activity leads to an inhibition of the cell-surface expression of both CCR5 and CXCR4, resulting in a significant inhibition of HIV-1 replication when PBMCs are challenged with the virus. In addition, we show that small single-stranded antisense RNAs can also be used to silence CCR5 and CXCR4 genes when delivered to PBMCs. This silencing is caused by selective degradation of receptor mRNAs.

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Sanders, Catherine M., Julius M. Cruse, and Robert E. Lewis. "Toll-like receptors, cytokines and HIV-1." Experimental and Molecular Pathology 84, no. 1 (February 2008): 31–36. http://dx.doi.org/10.1016/j.yexmp.2007.08.008.

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Weiss, R. A. "HIV Receptors and the Pathogenesis of AIDS." Science 272, no. 5270 (June 28, 1996): 1885. http://dx.doi.org/10.1126/science.272.5270.1885.

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Broder, Christopher C., and Dimiter S. Dimitrov. "HIV and the 7-Transmembrane Domain Receptors." Pathobiology 64, no. 4 (1996): 171–79. http://dx.doi.org/10.1159/000164032.

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Garzino-Demo, Alfredo, Anthony L. Devico, and Alfredo Garzino-Demo. "Chemokine Receptors and Chemokines in HIV Infection." Journal of Clinical Immunology 18, no. 4 (July 1998): 243–55. http://dx.doi.org/10.1023/a:1027329721892.

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Koirala, Janak, Alys Adamski, Lori Koch, Danielle Stueber, Mohammed El-Azizi, Nancy M. Khardori, Mahmood Ghassemi, and Richard M. Novak. "Interferon-Gamma Receptors in HIV-1 Infection." AIDS Research and Human Retroviruses 24, no. 8 (August 2008): 1097–102. http://dx.doi.org/10.1089/aid.2007.0261.

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Goldsmith, Mark A., and Robert W. Doms. "HIV entry: are all receptors created equal?" Nature Immunology 3, no. 8 (July 1, 2002): 709–10. http://dx.doi.org/10.1038/ni819.

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Lusso, Paolo. "A chemokine trap for HIV co-receptors." Nature Medicine 3, no. 10 (October 1997): 1074–75. http://dx.doi.org/10.1038/nm1097-1074.

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Achim, Cristian L., Virawudh Soontomniyomkij, Robert W. Dorsey, Wanda Wang, and Clayton A. Wiley. "NEUROTROPHIC FACTORS AND RECEPTORS IN HIV ENCEPHALITIS." Journal of Neuropathology and Experimental Neurology 57, no. 5 (May 1998): 490. http://dx.doi.org/10.1097/00005072-199805000-00095.

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Chen, Xin, Lu Yang, Ning Zhang, Jim A. Turpin, Robert W. Buckheit, Clay Osterling, Joost J. Oppenheim, and O. M. Zack Howard. "Shikonin, a Component of Chinese Herbal Medicine, Inhibits Chemokine Receptor Function and Suppresses Human Immunodeficiency Virus Type 1." Antimicrobial Agents and Chemotherapy 47, no. 9 (September 2003): 2810–16. http://dx.doi.org/10.1128/aac.47.9.2810-2816.2003.

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ABSTRACT Shikonin is a major component of zicao (purple gromwell, the dried root of Lithospermum erythrorhizon), a Chinese herbal medicine with various biological activities, including inhibition of human immunodeficiency virus (HIV) type 1 (HIV-1). G protein-coupled chemokine receptors are used by HIV-1 as coreceptors to enter the host cells. In this study, we assessed the effects of shikonin on chemokine receptor function and HIV-1 replication. The results showed that, at nanomolar concentrations, shikonin inhibited monocyte chemotaxis and calcium flux in response to a variety of CC chemokines (CCL2 [monocyte chemoattractant protein 1], CCL3 [macrophage inflammatory protein 1α], and CCL5 [regulated upon activation, normal T-cell expressed and secreted protein]), the CXC chemokine (CXCL12 [stromal cell-derived factor 1α]), and classic chemoattractants (formylmethionyl-leucine-phenylalanine and complement fraction C5a). Shikonin down-regulated surface expression of CCR5, a primary HIV-1 coreceptor, on macrophages to a greater degree than the other receptors (CCR1, CCR2, CXCR4, and the formyl peptide receptor) did. CCR5 mRNA expression was also down-regulated by the compound. Additionally, shikonin inhibited the replication of a multidrug-resistant strain and pediatric clinical isolates of HIV in human peripheral blood mononuclear cells, with 50% inhibitory concentrations (IC50s) ranging from 96 to 366 nM. Shikonin also effectively inhibited the replication of the HIV Ba-L isolate in monocytes/macrophages, with an IC50 of 470 nM. Our results suggest that the anti-HIV and anti-inflammatory activities of shikonin may be related to its interference with chemokine receptor expression and function. Therefore, shikonin, as a naturally occurring, low-molecular-weight pan-chemokine receptor inhibitor, constitutes a basis for the development of novel anti-HIV therapeutic agents.

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Farzan, Michael, Hyeryun Choe, Kathleen Martin, Luisa Marcon, Wolfgang Hofmann, Gunilla Karlsson, Ying Sun, et al. "Two Orphan Seven-Transmembrane Segment Receptors Which Are Expressed in CD4-positive Cells Support Simian Immunodeficiency Virus Infection." Journal of Experimental Medicine 186, no. 3 (August 4, 1997): 405–11. http://dx.doi.org/10.1084/jem.186.3.405.

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Clinical isolates of primate immunodeficiency viruses, including human immunodeficiency virus type 1 (HIV-1), enter target cells by sequential binding to CD4 and the chemokine receptor CCR5, a member of the seven-transmembrane receptor family. HIV-1 variants which use additional chemokine receptors are present in the central nervous system or emerge during the course of infection. Simian immunodeficiency viruses (SIV) have been shown to use CCR5 as a coreceptor, but no other receptors for these viruses have been identified. Here we show that two orphan seven-transmembrane segment receptors, gpr1 and gpr15, serve as coreceptors for SIV, and are expressed in human alveolar macrophages. The more efficient of these, gpr15, is also expressed in human CD4+ T lymphocytes and activated rhesus macaque peripheral blood mononuclear cells. The gpr15 and gpr1 proteins lack several hallmarks of chemokine receptors, but share with CCR5 an amino-terminal motif rich in tyrosine residues. These results underscore the potential diversity of seven-transmembrane segment receptors used as entry cofactors by primate immunodeficiency viruses, and may contribute to an understanding of viral variation and pathogenesis.

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del Real, Gustavo, Sonia Jiménez-Baranda, Rosa Ana Lacalle, Emilia Mira, Pilar Lucas, Concepción Gómez-Moutón, Ana C. Carrera, Carlos Martínez-A., and Santos Mañes. "Blocking of HIV-1 Infection by Targeting CD4 to Nonraft Membrane Domains." Journal of Experimental Medicine 196, no. 3 (August 5, 2002): 293–301. http://dx.doi.org/10.1084/jem.20020308.

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Human immunodeficiency virus (HIV)-1 infection depends on multiple lateral interactions between the viral envelope and host cell receptors. Previous studies have suggested that these interactions are possible because HIV-1 receptors CD4, CXCR4, and CCR5 partition in cholesterol-enriched membrane raft domains. We generated CD4 partitioning mutants by substituting or deleting CD4 transmembrane and cytoplasmic domains and the CD4 ectodomain was unaltered. We report that all CD4 mutants that retain raft partitioning mediate HIV-1 entry and CD4-induced Lck activation independently of their transmembrane and cytoplasmic domains. Conversely, CD4 ectodomain targeting to a nonraft membrane fraction results in a CD4 receptor with severely diminished capacity to mediate Lck activation or HIV-1 entry, although this mutant binds gp120 as well as CD4wt. In addition, the nonraft CD4 mutant inhibits HIV-1 X4 and R5 entry in a CD4+ cell line. These results not only indicate that HIV-1 exploits host membrane raft domains as cell entry sites, but also suggest new strategies for preventing HIV-1 infection.

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Journal articles on the topic 'HIV Receptors'

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