Journal articles: 'Neutralizing antibodies'

1

Vinson, Valda. "Protective neutralizing antibodies." Science 369, no. 6506 (August 20, 2020): 930.13–932. http://dx.doi.org/10.1126/science.369.6506.930-m.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Dempsey, Laurie A. "Zika-neutralizing antibodies." Nature Immunology 18, no. 6 (June 2017): 603. http://dx.doi.org/10.1038/ni.3762.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Bell, Elaine. "Neutralizing antibodies revisited." Nature Reviews Immunology 2, no. 6 (June 2002): 387. http://dx.doi.org/10.1038/nri833.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Muharemagic, D., A. S. Zamay, S. M. Ghobadloo, J. C. Bell, and M. V. Berezovski. "APTAMER-FACILITATED PROTECTION OF ONCOLYTIC VIRUS FROM NEUTRALIZING ANTIBODIES." Siberian Medical Review, no. 5 (2016): 116. http://dx.doi.org/10.20333/25000136-2016-5-116-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Kadkhoda, Kamran. "COVID ‐19: are neutralizing antibodies neutralizing enough?" Transfusion 60, no. 7 (June 3, 2020): 1602–3. http://dx.doi.org/10.1111/trf.15897.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Bjorkman, Pamela. "Neutralizing antibodies against coronaviruses." Microscopy and Microanalysis 27, S1 (July 30, 2021): 1112–13. http://dx.doi.org/10.1017/s1431927621004177.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Noronha, A. "Neutralizing antibodies to interferon." Neurology 68, Issue 24, Supplement 4 (June 11, 2007): S16—S22. http://dx.doi.org/10.1212/01.wnl.0000277705.63813.84.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Corti, Davide, and Antonio Lanzavecchia. "Broadly Neutralizing Antiviral Antibodies." Annual Review of Immunology 31, no. 1 (March 21, 2013): 705–42. http://dx.doi.org/10.1146/annurev-immunol-032712-095916.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Grauer, A., H. Reinel, R. Ziegler, and F. Raue. "Neutralizing Antibodies Against Calcitonin." Hormone and Metabolic Research 25, no. 09 (September 1993): 486–88. http://dx.doi.org/10.1055/s-2007-1002156.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

O'Connell, Nicola, and Bronwen Roper. "Testing for neutralizing antibodies." British Journal of Neuroscience Nursing 3, no. 2 (February 2007): 65–67. http://dx.doi.org/10.12968/bjnn.2007.3.2.23140.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Sok, Devin, Brian Moldt, and Dennis R. Burton. "SnapShot: Broadly Neutralizing Antibodies." Cell 155, no. 3 (October 2013): 728–728. http://dx.doi.org/10.1016/j.cell.2013.10.009.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Kulyk, Ya S. "EPITOPES IDENTIFICATION OF BROADLY NEUTRALIZING MONOCLONAL ANTIBODIES AGAINST Corynebacterium diphtheriae EXOTOXIN." Biotechnologia Acta 15, no. 4 (August 31, 2022): 37–40. http://dx.doi.org/10.15407/biotech15.04.037.

Full text

Abstract:

Background. Better and high-potency vaccines against diphtheria are urgently needed to provide broader protection against diverse strains and subtypes. Identification of novel broadly neutralizing epitopes targeted by protective antibodies could aid in such efforts. Aim. In this study we focused on the search of binding sites identification of anti diphtheria toxin monoclonal antibodies and their neutralizing activity to block binding of recombinant exotoxin derivates with host receptors. Methods. Vero cells were cultured in the complete RPMI-1640 medium under standard conditions and used for flow cytometry assay. Recombinant antigens and products of tryptic hydrolysis of CRM197 and SbB were characterized by Ni2+-NTA affinity chromatography and SDS-PAGE under reducing conditions with following ECL Western-Blot using several hybridomas clones of anti-diphtheria toxin monoclonal antibodies. Results. ECL western blot film results for clone 9.1-E11 showed the specific binding both to whole CRM197 molecule, and to almost all fragments of CRM197 formed as a result of limited proteolysis. In particular, a band corresponding to SbB in molecular weight can be identified. Thus, epitope region of the CRM197 molecule specific to 9.1-E1 mAbs is located within the structure of SbB. At the same time 16.4-E9 clone antibodies had high specificity to R-domain of SbB. In addition, both hybridoma clones antibodies have neutralizing activity against the DT binding subunit, which is a key factor in blocking between cell receptor and it ligand, C.diphtheriae exotoxin. Conclusions. The results obtained indicate that obtained antibodies are prospective for improving new diagnostic tools and therapeutic agents, which are used for treatment and understanding of the molecular mechanisms of diphtheria pathogenesis.

APA, Harvard, Vancouver, ISO, and other styles

13

Abdul Razak, Meerza, Bestha Lakshmi, Subramanyam Dasari, Pathan Shajahan Begum, Devarapogu Rajakumari, and Buddolla Viswanath. "Neutralizing Antibodies in HIV Treatment." Current Biotechnology 5, no. 1 (February 2, 2016): 11–27. http://dx.doi.org/10.2174/2211550105666151125220558.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Cully, Megan. "Broadly neutralizing anti-coronavirus antibodies." Nature Reviews Drug Discovery 20, no. 9 (July 27, 2021): 665. http://dx.doi.org/10.1038/d41573-021-00128-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Cutter, G. "Statistical issues in neutralizing antibodies." Neurology 61, Issue 9, Supplement 5 (November 10, 2003): S38—S39. http://dx.doi.org/10.1212/01.wnl.0000092365.14383.56.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Brown, Matthew. "Preventing escape from neutralizing antibodies." Nature Reviews Immunology 20, no. 9 (July 31, 2020): 521. http://dx.doi.org/10.1038/s41577-020-00414-w.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Uhl, Lion F. K., and Anne Chauveau. "Neutralizing antibodies in convalescent patients." Nature Reviews Immunology 20, no. 8 (June 12, 2020): 460. http://dx.doi.org/10.1038/s41577-020-0370-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Arendrup, Maiken, Claus Nielsen, John-Erik Stig Hansen, Court Pedersen, Lars Mathiesen, and Jens Ole Nielsen. "Autologous HIV-1 Neutralizing Antibodies." JAIDS Journal of Acquired Immune Deficiency Syndromes 5, no. 3 (March 1992): 303???307. http://dx.doi.org/10.1097/00126334-199203000-00012.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Athavale, Prachi, Virendra Athavale, Poonam Suryawanshi, Kishor Khillare, and Srikanth Tripathy. "Neutralizing Antibodies against SARS-CoV2." Medical Journal of Dr. D.Y. Patil Vidyapeeth 17, no. 1 (June 2, 2023): 9–18. http://dx.doi.org/10.4103/mjdrdypu.mjdrdypu_819_22.

Full text

Abstract:

ABSTRACT Coronavirus disease 2019 (COVID-19) is an illness due to a novel coronavirus which is Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2). Though this virus is recently identified in 2019, it is closely related to other coronaviruses namely SARS-CoV and MERS-CoV. A neutralizing antibody (NAb) is defined as an antibody that is responsible for defending cells from pathogens. They are produced naturally by the body as part of its immune response, and their production is triggered by both infections and vaccinations against infections. Articles published databases of PubMed, Embase, SCOPUS and Cochrane were studied. The keywords used by authors were ‘SARS-CoV-2”, “COVID-19”, “seroprevalence”, “convalescent plasma”, “neutralizing antibodies”, “antibodies”, “antibody dependent enhancement”. There is great importance of neutralizing antibodies in SARS-CoV-2 infection. Most of the patients who suffered with SARS-CoV-2 develop different titers of NAbs at an interval of 14 and 20 days after infection. When all three immunoglobulin classes namely IgG, IgM, and IgA are formed and work synergistically, the maximum neutralization activity against SARS-CoV-2 is observed. The reduction in NAb titre occurs in two phases. There are many new cases of re-infections reported from all over the world which suggest that immunity against SARS-CoV-2 is short lasting and incomplete. Vaccines play an important role in preventing deaths and hospitalization caused by infectious diseases and contributes to controlling the spread of the disease, thus their impact on infection and serious illness is significant.

APA, Harvard, Vancouver, ISO, and other styles

20

Misra, Puneet, Shashi Kant, Randeep Guleria, Sanjay K. Rai, Abhishek Jaiswal, Suprakash Mandal, Guruprasad R. Medigeshi, et al. "Antibody Response to SARS-CoV-2 among COVID-19 Confirmed Cases and Correlates with Neutralizing Assay in a Subgroup of Patients in Delhi National Capital Region, India." Vaccines 10, no. 8 (August 14, 2022): 1312. http://dx.doi.org/10.3390/vaccines10081312.

Full text

Abstract:

Background: The plaque reduction neutralization test (PRNT) is the gold standard to detect the neutralizing capacity of serum antibodies. Neutralizing antibodies confer protection against further infection. The present study measured the antibody level against SARS-CoV-2 among laboratory-confirmed COVID-19 cases and evaluated whether the presence of anti-SARS-CoV-2 antibodies indicates virus neutralizing capacity. Methods: One hundred COVID-19 confirmed cases were recruited. Their sociodemographic details and history of COVID-19 vaccination, contact with positive COVID-19 cases, and symptoms were ascertained using a self-developed semi-structured interview schedule. Serum samples of the participants were collected within three months from the date of the positive report of COVID-19. The presence of anti-SARS-CoV-2 antibodies (IgA, IgG and IgM antibodies), receptor binding domain antibodies (anti-RBD), and neutralizing antibodies were measured. Findings: Almost all the participants had anti-SARS-CoV-2 antibodies (IgA, IgG and IgM) (99%) and anti-RBD IgG antibodies (97%). However, only 69% had neutralizing antibodies against SARS-CoV-2. Anti-RBD antibody levels were significantly higher among participants having neutralizing antibodies compared with those who did not. Interpretation: The present study highlights that the presence of antibodies against SARS-CoV-2, or the presence of anti-RBD antibodies does not necessarily imply the presence of neutralizing antibodies.

APA, Harvard, Vancouver, ISO, and other styles

21

Keck, Zhen-yong, Christine Girard-Blanc, Wenyan Wang, Patrick Lau, Adam Zuiani, Felix A. Rey, Thomas Krey, Michael S. Diamond, and Steven K. H. Foung. "Antibody Response to Hypervariable Region 1 Interferes with Broadly Neutralizing Antibodies to Hepatitis C Virus." Journal of Virology 90, no. 6 (January 6, 2016): 3112–22. http://dx.doi.org/10.1128/jvi.02458-15.

Full text

Abstract:

ABSTRACTHypervariable region 1 (HVR1) (amino acids [aa] 384 to 410) on the E2 glycoprotein of hepatitis C virus contributes to persistent infection by evolving escape mutations that attenuate binding of inhibitory antibodies and by blocking access of broadly neutralizing antibodies to their epitopes. A third proposed mechanism of immune antagonism is that poorly neutralizing antibodies binding to HVR1 interfere with binding of other superior neutralizing antibodies. Epitope mapping of human monoclonal antibodies (HMAbs) that bind to an adjacent, conserved domain on E2 encompassing aa 412 to 423 revealed two subsets, designated HC33 HMAbs. While both subsets have contact residues within aa 412 to 423, alanine-scanning mutagenesis suggested that one subset, which includes HC33.8, has an additional contact residue within HVR1. To test for interference of anti-HVR1 antibodies with binding of antibodies to aa 412 to 423 and other E2 determinants recognized by broadly neutralizing HMAbs, two murine MAbs against HVR1 (H77.16) and aa 412 to 423 (H77.39) were studied. As expected, H77.39 inhibited the binding of all HC33 HMAbs. Unexpectedly, H77.16 also inhibited the binding of both subsets of HC33 HMAbs. This inhibition also was observed against other broadly neutralizing HMAbs to epitopes outside aa 412 to 423. Combination antibody neutralization studies by the median-effect analysis method with H77.16 and broadly reactive HMAbs revealed antagonism between these antibodies. Structural studies demonstrated conformational flexibility in this antigenic region, which supports the possibility of anti-HVR1 antibodies hindering the binding of broadly neutralizing MAbs. These findings support the hypothesis that anti-HVR1 antibodies can interfere with a protective humoral response against HCV infection.IMPORTANCEHVR1 contributes to persistent infection by evolving mutations that escape from neutralizing antibodies to HVR1 and by shielding broadly neutralizing antibodies from their epitopes. This study provides insight into a new immune antagonism mechanism by which the binding of antibodies to HVR1 blocks the binding and activity of broadly neutralizing antibodies to HCV. Immunization strategies that avoid the induction of HVR1 antibodies should increase the inhibitory activity of broadly neutralizing anti-HCV antibodies elicited by candidate vaccines.

APA, Harvard, Vancouver, ISO, and other styles

22

Tsai, Wen-Yang, Anna Durbin, Jih-Jin Tsai, Szu-Chia Hsieh, Stephen Whitehead, and Wei-Kung Wang. "Complexity of Neutralizing Antibodies against Multiple Dengue Virus Serotypes after Heterotypic Immunization and Secondary Infection Revealed by In-Depth Analysis of Cross-Reactive Antibodies." Journal of Virology 89, no. 14 (May 13, 2015): 7348–62. http://dx.doi.org/10.1128/jvi.00273-15.

Full text

Abstract:

ABSTRACTThe four serotypes of dengue virus (DENV) cause the most important and rapidly emerging arboviral diseases in humans. The recent phase 2b and 3 studies of a tetravalent dengue vaccine reported a moderate efficacy despite the presence of neutralizing antibodies, highlighting the need for a better understanding of neutralizing antibodies in polyclonal human sera. Certain type-specific (TS) antibodies were recently discovered to account for the monotypic neutralizing activity and protection after primary DENV infection. The nature of neutralizing antibodies after secondary DENV infection remains largely unknown. In this study, we examined sera from 10 vaccinees with well-documented exposure to first and second DENV serotypes through heterotypic immunization with live-attenuated vaccines. Higher serum IgG avidities to both exposed and nonexposed serotypes were found after secondary immunization than after primary immunization. Using a two-step depletion protocol to remove different anti-envelope antibodies, including group-reactive (GR) and complex-reactive (CR) antibodies separately, we found GR and CR antibodies together contributed to more than 50% of neutralizing activities against multiple serotypes after secondary immunization. Similar findings were demonstrated in patients after secondary infection. Anti-envelope antibodies recognizing previously exposed serotypes consisted of a large proportion of GR antibodies, CR antibodies, and a small proportion of TS antibodies, whereas those recognizing nonexposed serotypes consisted of GR and CR antibodies. These findings have implications for sequential heterotypic immunization or primary immunization of DENV-primed individuals as alternative strategies for DENV vaccination. The complexity of neutralizing antibodies after secondary infection provides new insights into the difficulty of their application as surrogates of protection.IMPORTANCEThe four serotypes of dengue virus (DENV) are the leading cause of arboviral diseases in humans. Despite the presence of neutralizing antibodies, a moderate efficacy was recently reported in phase 2b and 3 trials of a dengue vaccine; a better understanding of neutralizing antibodies in polyclonal human sera is urgently needed. We studied vaccinees who received heterotypic immunization of live-attenuated vaccines, as they were known to have received the first and second DENV serotype exposures. We found anti-envelope antibodies consist of group-reactive (GR), complex-reactive (CR), and type-specific (TS) antibodies, and that both GR and CR antibodies contribute significantly to multitypic neutralizing activities after secondary DENV immunization. These findings have implications for alternative strategies for DENV vaccination. Certain TS antibodies were recently discovered to contribute to the monotypic neutralizing activity and protection after primary DENV infection; our findings of the complexity of neutralizing activities after secondary immunization/infection provide new insights for neutralizing antibodies as surrogates of protection.

APA, Harvard, Vancouver, ISO, and other styles

23

Cao, Yunlong, Jing Wang, Fanchong Jian, Tianhe Xiao, Weiliang Song, Ayijiang Yisimayi, Weijin Huang, et al. "Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies." Nature 602, no. 7898 (December 23, 2021): 657–63. http://dx.doi.org/10.1038/s41586-021-04385-3.

Full text

Abstract:

AbstractThe SARS-CoV-2 B.1.1.529 (Omicron) variant contains 15 mutations of the receptor-binding domain (RBD). How Omicron evades RBD-targeted neutralizing antibodies requires immediate investigation. Here we use high-throughput yeast display screening1,2 to determine the profiles of RBD escaping mutations for 247 human anti-RBD neutralizing antibodies and show that the neutralizing antibodies can be classified by unsupervised clustering into six epitope groups (A–F)—a grouping that is highly concordant with knowledge-based structural classifications3–5. Various single mutations of Omicron can impair neutralizing antibodies of different epitope groups. Specifically, neutralizing antibodies in groups A–D, the epitopes of which overlap with the ACE2-binding motif, are largely escaped by K417N, G446S, E484A and Q493R. Antibodies in group E (for example, S309)6 and group F (for example, CR3022)7, which often exhibit broad sarbecovirus neutralizing activity, are less affected by Omicron, but a subset of neutralizing antibodies are still escaped by G339D, N440K and S371L. Furthermore, Omicron pseudovirus neutralization showed that neutralizing antibodies that sustained single mutations could also be escaped, owing to multiple synergetic mutations on their epitopes. In total, over 85% of the tested neutralizing antibodies were escaped by Omicron. With regard to neutralizing-antibody-based drugs, the neutralization potency of LY-CoV016, LY-CoV555, REGN10933, REGN10987, AZD1061, AZD8895 and BRII-196 was greatly undermined by Omicron, whereas VIR-7831 and DXP-604 still functioned at a reduced efficacy. Together, our data suggest that infection with Omicron would result in considerable humoral immune evasion, and that neutralizing antibodies targeting the sarbecovirus conserved region will remain most effective. Our results inform the development of antibody-based drugs and vaccines against Omicron and future variants.

APA, Harvard, Vancouver, ISO, and other styles

24

McCoy, Laura E., and Robin A. Weiss. "Neutralizing antibodies to HIV-1 induced by immunization." Journal of Experimental Medicine 210, no. 2 (February 11, 2013): 209–23. http://dx.doi.org/10.1084/jem.20121827.

Full text

Abstract:

Most neutralizing antibodies act at the earliest steps of viral infection and block interaction of the virus with cellular receptors to prevent entry into host cells. The inability to induce neutralizing antibodies to HIV has been a major obstacle to HIV vaccine research since the early days of the epidemic. However, in the past three years, the definition of a neutralizing antibody against HIV has been revolutionized by the isolation of extremely broad and potent neutralizing antibodies from HIV-infected individuals. Considerable hurdles remain for inducing neutralizing antibodies to a protective level after immunization. Meanwhile, novel technologies to bypass the induction of antibodies are being explored to provide prophylactic antibody-based interventions. This review addresses the challenge of inducing HIV neutralizing antibodies upon immunization and considers notable recent advances in the field. A greater understanding of the successes and failures for inducing a neutralizing response upon immunization is required to accelerate the development of an effective HIV vaccine.

APA, Harvard, Vancouver, ISO, and other styles

25

Seiler, Peter, Ulrich Kalinke, Thomas Rülicke, Etienne M. Bucher, Christian Böse, Rolf M. Zinkernagel, and Hans Hengartner. "Enhanced Virus Clearance by Early Inducible Lymphocytic Choriomeningitis Virus-Neutralizing Antibodies in Immunoglobulin-Transgenic Mice." Journal of Virology 72, no. 3 (March 1, 1998): 2253–58. http://dx.doi.org/10.1128/jvi.72.3.2253-2258.1998.

Full text

Abstract:

ABSTRACT Following infection of mice with lymphocytic choriomeningitis virus (LCMV), virus-neutralizing antibodies appear late, after 30 to 60 days. Such neutralizing antibodies play an important role in protection against reinfection. To analyze whether a neutralizing antibody response which developed earlier could contribute to LCMV clearance during the acute phase of infection, we generated transgenic mice expressing LCMV-neutralizing antibodies. Transgenic mice expressing the immunoglobulin μ heavy chain of the LCMV-neutralizing monoclonal antibody KL25 (H25 transgenic mice) mounted LCMV-neutralizing immunoglobulin M (IgM) serum titers within 8 days after infection. This early inducible LCMV-neutralizing antibody response significantly improved the host’s capacity to clear the infection and did not cause an enhancement of disease after intracerebral (i.c.) LCMV infection. In contrast, mice which had been passively administered LCMV-neutralizing antibodies and transgenic mice exhibiting spontaneous LCMV-neutralizing IgM serum titers (HL25 transgenic mice expressing the immunoglobulin μ heavy and the κ light chain) showed an enhancement of disease after i.c. LCMV infection. Thus, early-inducible LCMV-neutralizing antibodies can contribute to viral clearance in the acute phase of the infection and do not cause antibody-dependent enhancement of disease.

APA, Harvard, Vancouver, ISO, and other styles

26

Moore, Penny L. "The Neutralizing Antibody Response to the HIV-1 Env Protein." Current HIV Research 16, no. 1 (April 19, 2018): 21–28. http://dx.doi.org/10.2174/1570162x15666171124122044.

Full text

Abstract:

Background: A vaccine able to elicit broadly neutralizing antibodies capable of blocking infection by global viruses has not been achieved, and remains a key public health challenge.Objective: During infection, a robust strain-specific neutralizing response develops in most people, but only a subset of infected people develop broadly neutralizing antibodies. Understanding how and why these broadly neutralizing antibodies develop has been a focus of the HIV-1 vaccine field for many years, and has generated extraordinary insights into the neutralizing response to HIV-1 infection.Results: This review describes the features, targets and developmental pathways of early strainspecific antibodies and later broadly neutralizing antibodies, and explores the reasons such broad antibodies are not more commonly elicited during infection.Conclusion: The insights from these studies have been harnessed for the development of pioneering new vaccine approaches that seek to drive B cell maturation towards breadth. Overall, this review describes how findings from infected donors have impacted on active and passive immunization approaches that seek to prevent HIV-1 infection.

APA, Harvard, Vancouver, ISO, and other styles

27

Montefiori, David C., Keith A. Reimann, Michael S. Wyand, Kelledy Manson, Mark G. Lewis, Ronald G. Collman, Joseph G. Sodroski, Dani P. Bolognesi, and Norman L. Letvin. "Neutralizing Antibodies in Sera from Macaques Infected with Chimeric Simian-Human Immunodeficiency Virus Containing the Envelope Glycoproteins of either a Laboratory-Adapted Variant or a Primary Isolate of Human Immunodeficiency Virus Type 1." Journal of Virology 72, no. 4 (April 1, 1998): 3427–31. http://dx.doi.org/10.1128/jvi.72.4.3427-3431.1998.

Full text

Abstract:

ABSTRACT The magnitude and breadth of neutralizing antibodies raised in response to infection with chimeric simian-human immunodeficiency virus (SHIV) in rhesus macaques were evaluated. Infection with either SHIV-HXB2, SHIV-89.6, or SHIV-89.6PD raised high-titer neutralizing antibodies to the homologous SHIV (SHIV-89.6P in the case of SHIV-89.6PD-infected animals) and significant titers of neutralizing antibodies to human immunodeficiency virus type 1 (HIV-1) strains MN and SF-2. With few exceptions, however, titers of neutralizing antibodies to heterologous SHIV were low or undetectable. The antibodies occasionally neutralized heterologous primary isolates of HIV-1; these antibodies required >40 weeks of infection to reach detectable levels. Notable was the potent neutralization of the HIV-1 89.6 primary isolate by serum samples from SHIV-89.6-infected macaques. These results demonstrate that SHIV-HXB2, SHIV-89.6, and SHIV-89.6P possess highly divergent, strain-specific neutralization epitopes. The results also provide insights into the requirements for raising neutralizing antibodies to primary isolates of HIV-1.

APA, Harvard, Vancouver, ISO, and other styles

28

Gneiss, C., P. Tripp, R. Ehling, M. Khalil, A. Lutterotti, R. Egg, I. Mayringer, et al. "Interferon-β antibodies have a higher affinity in patients with neutralizing antibodies compared to patients with non-neutralizing antibodies." Journal of Neuroimmunology 174, no. 1-2 (May 2006): 174–79. http://dx.doi.org/10.1016/j.jneuroim.2006.01.017.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Mbulawa, Zizipho Z. A., Anna-Lise Williamson, Debbie Stewart, Jo-Ann S. Passmore, Lynette Denny, Bruce Allan, and Dianne J. Marais. "Association of serum and mucosal neutralizing antibodies to human papillomavirus type 16 (HPV-16) with HPV-16 infection and cervical disease." Journal of General Virology 89, no. 4 (April 1, 2008): 910–14. http://dx.doi.org/10.1099/vir.0.83458-0.

Full text

Abstract:

We investigated neutralizing antibodies to human papillomavirus type 16 (HPV-16) in serum and cervical washes from 84 women with normal cytology or cervical disease. Serum neutralizing antibodies were detected in 78 % of women infected at the cervix with HPV-16, compared with 35 % (P=0.002) of women infected with HPV-16-related types (α9 HPV types), 14 % (P<0.0001) of women infected with HPV-16 non-related types and none of HPV-uninfected women. A significant correlation between HPV-16 infection and serum HPV-16-neutralizing antibodies was observed (r s=0.97; P=0.032). Cervical neutralizing antibodies were detected in 38 % of women with HPV-16 infection and in 17 % of women infected with the HPV-16-related type HPV-31. Cervical neutralizing antibodies correlated with HPV-16 infection (r s=0.95; P=0.08), but not with cervical disease. Serum and cervical HPV-16 antibody responses were not affected significantly by human immunodeficiency virus type 1 infection. In conclusion, serum and cervical HPV-16-neutralizing antibodies were found to correlate with HPV-16 infection, but not with cervical disease.

APA, Harvard, Vancouver, ISO, and other styles

30

Akhras, Sami, Marie-Luise Herrlein, Fabian Elgner, Thomas Holzhauser, and Eberhard Hildt. "ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization." Viruses 11, no. 8 (August 13, 2019): 748. http://dx.doi.org/10.3390/v11080748.

Full text

Abstract:

Infection with Zika virus (ZIKV) came first to public attention after it was found to be associated with congenital microcephaly during the outbreak in Brazil (2015–2016). Diagnosis of ZIKV suffers from extensive cross-reactivity with other Flaviviruses, which are circulating in many ZIKV epidemic areas. Due to the fatal outcome of ZIKV infection during pregnancy, detailed knowledge about neutralizing and non-neutralizing epitopes is crucial for the development of robust detection systems of protective antibodies. Therefore, additional information about ZIKV immunogenicity and antibody response is required. In this project, we report the production, purification and characterization of six different polyclonal antibodies against ZIKV envelope (E) protein. The produced antibodies bind to isolated ZIKV E protein as well as to the surface of ZIKV particles, interestingly without being potently neutralizing. Surface plasmon resonance measurement showed that these antibodies bind with high affinity to ZIKV E protein. Epitope mapping revealed that the epitopes are distributed among the three ZIKV E domains with seven binding sites. These identified binding sites overlap only partially with the previously described epitopes recognized by neutralizing antibodies, which is in accordance with their lack of potent neutralizing activity. Additionally, these antibodies showed neither cross-reactivity nor potent neutralizing activity against West Nile virus, a related flavivirus. The gained set of data helps to extend our understanding about the distribution of neutralizing and non-/weak-neutralizing epitopes in ZIKV E protein, and provides a rationale for ZIKV vaccine design and development of robust detection assays for neutralizing antibodies.

APA, Harvard, Vancouver, ISO, and other styles

31

Brown, Justin, Kristin Skoland, Heather Kittrell, Josh Ellingson, Paul Thomas, Chelsea Ruston, David Baum, and Locke Karriker. "Longitudinal and Cross-Sectional Evaluation of Two Commercial Swine Breeding Herds to Characterize Neutralizing Antibody Levels following Porcine Epidemic Diarrhea Virus Outbreaks." Viruses 16, no. 3 (February 21, 2024): 324. http://dx.doi.org/10.3390/v16030324.

Full text

Abstract:

Neutralizing antibodies to Porcine Epidemic Diarrhea Virus (PEDV) can be detected by 3 weeks post-infection and remain detectable through at least 24 weeks post-infection. The objective of this study was to evaluate the levels of neutralizing antibodies in sow and piglet serum and sow milk to determine the duration of neutralizing antibodies following PEDV outbreaks. Two farms were selected for the study following outbreaks of PEDV. Monthly, cohorts of sows were sampled and followed through two farrowings. Following each farrowing, samples from piglets and milk were collected. Samples were evaluated for PEDV-neutralizing antibodies by a high-throughput fluorescent neutralization assay. Although neutralizing antibodies to PEDV can be detected throughout 15 months post-outbreak, a decrease in circulating neutralizing antibody levels is noted in farms beginning at six months post-outbreak. With decreasing levels, farms may become more vulnerable to PEDV outbreaks, and practitioners can focus on this time window to implement intervention strategies.

APA, Harvard, Vancouver, ISO, and other styles

32

Battegay, M., D. Moskophidis, H. Waldner, M. A. Bründler, W. P. Fung-Leung, T. W. Mak, H. Hengartner, and R. M. Zinkernagel. "Impairment and delay of neutralizing antiviral antibody responses by virus-specific cytotoxic T cells." Journal of Immunology 151, no. 10 (November 15, 1993): 5408–15. http://dx.doi.org/10.4049/jimmunol.151.10.5408.

Full text

Abstract:

Abstract After infection with some viruses that tend to persist, neutralizing antibodies are generated rather late, i.e., after 1 to 3 mo. This has been observed for HIV, Hepatitis B infection in man, or after infection with lymphocytic choriomeningitis virus (LCMV) in mice. In contrast, nonneutralizing antibodies to LCMV are generated by day 7 and reach high titers by day 10. This study attempts to evaluate reasons for late and low titered neutralizing antibody responses. After a primary infection with low doses (10(2) plaque forming units) of the poorly cytopathic LCMV-WE, neutralizing antibodies were rarely produced at detectable levels before days 60 to 120. In vivo depletion of CD8+ CTL led to a marked enhancement and acceleration of kinetics of the neutralizing antibody response. In contrast, nonneutralizing antibodies, including those specific for LCMV-GP carrying the neutralizing determinant, were detectable very early, i.e., 4 to 7 days after infection, with maximum titers usually by day 10 irrespective of the presence or absence of CTL. Mice completely lacking CD8+ T cells because of deletion by homologous recombination (CD8-/-) also exhibited neutralizing antibodies early by day 10 to 20, and by day 120 reached very high titers. The neurotropic isolate LCMV-ARMSTRONG induced low but significant titers of neutralizing antibodies relatively early (i.e., by days 7 to 10), whereas the lympho-viscerotrope mutant virus LCMV-ARMSTRONG Cl-13 did not. Early and effective CTL responses causing immunopathology (and immunosuppression) correlated with the absence of neutralizing antibodies. The discrepancy between the CTL-dependent inhibition of neutralizing versus unimpaired anti-GP ELISA responses cannot be explained by different Ag doses alone. Additionally, it may reflect different kinetics of the responses, whereby the later neutralizing responses possibly requiring IgG affinity maturation may be more susceptible to general immunosuppression; also B cells expressing neutralizing receptors, but not those with antibodies binding GP (or NP), may be actively infected, therefore they present viral peptides on class I MHC Ag and may become targets for anti-LCMV-specific CTL.

APA, Harvard, Vancouver, ISO, and other styles

33

Ranasinghe, Srinika, Damien Z. Soghoian, Madelene Lindqvist, Musie Ghebremichael, Faith Donaghey, Mary Carrington, Michael S. Seaman, Daniel E. Kaufmann, Bruce D. Walker, and Filippos Porichis. "HIV-1 Antibody Neutralization Breadth Is Associated with Enhanced HIV-Specific CD4+T Cell Responses." Journal of Virology 90, no. 5 (December 9, 2015): 2208–20. http://dx.doi.org/10.1128/jvi.02278-15.

Full text

Abstract:

ABSTRACTAntigen-specific CD4+T helper cell responses have long been recognized to be a critical component of effective vaccine immunity. CD4+T cells are necessary to generate and maintain humoral immune responses by providing help to antigen-specific B cells for the production of antibodies. In HIV infection, CD4+T cells are thought to be necessary for the induction of Env-specific broadly neutralizing antibodies. However, few studies have investigated the role of HIV-specific CD4+T cells in association with HIV neutralizing antibody activity in vaccination or natural infection settings. Here, we conducted a comprehensive analysis of HIV-specific CD4+T cell responses in a cohort of 34 untreated HIV-infected controllers matched for viral load, with and without neutralizing antibody breadth to a panel of viral strains. Our results show that the breadth and magnitude of Gag-specific CD4+T cell responses were significantly higher in individuals with neutralizing antibodies than in those without neutralizing antibodies. The breadth of Gag-specific CD4+T cell responses was positively correlated with the breadth of neutralizing antibody activity. Furthermore, the breadth and magnitude of gp41-specific, but not gp120-specific, CD4+T cell responses were significantly elevated in individuals with neutralizing antibodies. Together, these data suggest that robust Gag-specific CD4+T cells and, to a lesser extent, gp41-specific CD4+T cells may provide important intermolecular help to Env-specific B cells that promote the generation or maintenance of Env-specific neutralizing antibodies.IMPORTANCEOne of the earliest discoveries related to CD4+T cell function was their provision of help to B cells in the development of antibody responses. Yet little is known about the role of CD4+T helper responses in the setting of HIV infection, and no studies to date have evaluated the impact of HIV-specific CD4+T cells on the generation of antibodies that can neutralize multiple different strains of HIV. Here, we addressed this question by analyzing HIV-specific CD4+T cell responses in untreated HIV-infected persons with and without neutralizing antibodies. Our results indicate that HIV-infected persons with neutralizing antibodies have significantly more robust CD4+T cell responses targeting Gag and gp41 proteins than individuals who lack neutralizing antibodies. These associations suggest that Gag- and gp41-specific CD4+T cell responses may provide robust help to B cells for the generation or maintenance of neutralizing antibodies in natural HIV-infection.

APA, Harvard, Vancouver, ISO, and other styles

34

Chen, Chin-Ho, Lei Jin, Chongbin Zhu, Sonia Holz-Smith, and Thomas J. Matthews. "Induction and Characterization of Neutralizing Antibodies against a Human Immunodeficiency Virus Type 1 Primary Isolate." Journal of Virology 75, no. 14 (July 15, 2001): 6700–6704. http://dx.doi.org/10.1128/jvi.75.14.6700-6704.2001.

Full text

Abstract:

ABSTRACT Chimpanzees infected with the primary isolate DH012 mount potent neutralizing antibodies. This DH012 neutralizing activity is highly strain specific. Immune sera from guinea pigs immunized with recombinant DH012 gp120 could also neutralize this primary isolate. The neutralizing activity in chimpanzee and guinea pig sera against wild-type DH012 appears to be independent of a linear epitope in the V3 region of gp120. Interestingly, the neutralization escape mutant derived from growing DH012 in the presence of the potent neutralizing chimpanzee serum is at least 50-fold more sensitive than wild-type DH012 to neutralization by guinea pig immune sera. The unusually potent neutralizing activity against the DH012 neutralization-resistant virus is due to the presence of anti-V3 antibodies in guinea pig sera. These results suggested that recombinant gp120 could induce neutralizing antibodies against primary isolate DH012. The V3 of wild-type DH012 is poorly immunogenic in infected chimpanzees and is not accessible to neutralizing V3 antibodies. It is likely that this cryptic V3 region became exposed when the virus escaped the neutralizing activity of the chimpanzee serum.

APA, Harvard, Vancouver, ISO, and other styles

35

Bowers, Charles, Daniel T. Mytych, Tatiana Lawrence, Kejia Wang, Troy E. Barger, Melissa Eisen, Carolyn M. Bennett, and Michael D. Tarantino. "Assessment of romiplostim immunogenicity in pediatric patients in clinical trials and in a global postmarketing registry." Blood Advances 5, no. 23 (December 2, 2021): 4969–79. http://dx.doi.org/10.1182/bloodadvances.2021005105.

Full text

Abstract:

Abstract Development of first-generation thrombopoietins (TPOs) was halted due to antibodies that neutralized endogenous TPO, causing protracted thrombocytopenia in some patients. The second-generation TPO receptor agonist romiplostim, having no homology to TPO, was developed to circumvent potential immunogenicity. We examined the development of binding and neutralizing antibodies to romiplostim and TPO among pediatric patients with primary immune thrombocytopenia (ITP) in 5 clinical trials and a global postmarketing registry. In the trials, 25 of 280 (8.9%) patients developed anti-romiplostim binding antibodies. The first positive result was detected 67 weeks (median) after romiplostim treatment was initiated. The median romiplostim dose was 8 µg/kg, and the median platelet count was 87 × 109/L. Most patients who developed anti-romiplostim binding antibodies (18 of 25 [72%]) had ≥90% of platelet assessments showing a response. Anti-romiplostim neutralizing antibodies developed in 8 of 280 (2.9%) patients. The development of anti-romiplostim neutralizing antibodies was unrelated to the romiplostim dose, and most patients who developed the antibodies (7 of 8 [88%]) had platelet response. Nine of 279 (3.2%) patients developed anti-TPO binding antibodies, and 1 (0.4%) developed transient anti-TPO neutralizing antibodies. In 8 patients who developed anti-romiplostim neutralizing antibodies, no TPO cross-reactivity was observed. In the postmarketing registry, 3 of 19 (15.8%) patients developed anti-romiplostim binding antibodies; 1 (5.3%) patient developed anti-romiplostim neutralizing antibodies. These results suggest that immunogenicity to romiplostim occurs infrequently in pediatric patients with ITP and is generally not associated with loss of platelet response or other negative clinical sequelae.

APA, Harvard, Vancouver, ISO, and other styles

36

Hocher, Berthold, Anne Schönbrunn, Xin Chen, Bernhard K. Krämer, and Volker von Baehr. "Outliers Matter—Correlation between S1 IgG SARS-CoV-2 Antibodies and Neutralizing SARS-CoV-2 Antibodies." Microorganisms 10, no. 10 (October 19, 2022): 2067. http://dx.doi.org/10.3390/microorganisms10102067.

Full text

Abstract:

Vaccination against the SARS-CoV-2 virus or infection with SARS-CoV-2 will lead to the development of IgG antibodies against the S1 protein of the SARS-CoV-2 virus. However, even despite having high levels of IgG antibodies against the S1 protein of the SARS-CoV-2 virus, (re-)infection may occur. We thus examined 2994 consecutive blood samples of outpatients from the Berlin-Brandenburg area in Germany in which IgG antibodies against the S1 protein of the SARS-CoV-2 virus as well as neutralizing SARS-CoV-2 virus antibodies were determined from the same sample. When analyzing the entire study population (2994 outpatients), we saw that S1 IgG antibodies (women: 223.98 ± 3.81; men: 207.80 ± 4.59; p = 0.014) and neutralizing antibodies (women: 66.65 ± 0.82; men: 62.88 ± 1.01; p = 0.021) are slightly higher in women than in men. Curve fitting revealed a good non-linear relationship between S1 IgG and neutralizing SARS-CoV-2 antibodies. However, 51 out of the 2994 blood samples from individual subjects were positive with regard to the neutralizing antibodies and at the same time negative for S1 IgG antibodies, and 112 out of the 2994 blood samples from individual subjects were negative with regard to the neutralizing antibodies and at the same time positive for S1 IgG antibodies. In conclusion, our study shows that there is a relevant number of patients who, despite developing significant titers of S1 antibodies, do not have relevant amounts of neutralizing antibody titers and are probably at high risk of (re-)infection.

APA, Harvard, Vancouver, ISO, and other styles

37

Caillat, Christophe, Delphine Guilligay, Guidenn Sulbaran, and Winfried Weissenhorn. "Neutralizing Antibodies Targeting HIV-1 gp41." Viruses 12, no. 11 (October 23, 2020): 1210. http://dx.doi.org/10.3390/v12111210.

Full text

Abstract:

HIV-1 vaccine research has obtained an enormous boost since the discovery of many broadly neutralizing antibodies (bnAbs) targeting all accessible sites on the HIV-1 envelope glycoprotein (Env). This in turn facilitated high-resolution structures of the Env glycoprotein in complex with bnAbs. Here we focus on gp41, its highly conserved heptad repeat region 1 (HR1), the fusion peptide (FP) and the membrane-proximal external region (MPER). Notably, the broadest neutralizing antibodies target MPER. Both gp41 HR1 and MPER are only fully accessible once receptor-induced conformational changes have taken place, although some studies suggest access to MPER in the close to native Env conformation. We summarize the data on the structure and function of neutralizing antibodies targeting gp41 HR1, FP and MPER and we review their access to Env and their complex formation with gp41 HR1, MPER peptides and FP within native Env. We further discuss MPER bnAb binding to lipids and the role of somatic mutations in recognizing a bipartite epitope composed of the conserved MPER sequence and membrane components. The problematic of gp41 HR1 access and MPER bnAb auto- and polyreactivity is developed in the light of inducing such antibodies by vaccination.

APA, Harvard, Vancouver, ISO, and other styles

38

Borowski, Christine. "Membrane fishing for HIV-neutralizing antibodies." Nature Biotechnology 30, no. 9 (September 2012): 841. http://dx.doi.org/10.1038/nbt.2367.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Haynes, B. F., and L. Verkoczy. "Host Controls of HIV Neutralizing Antibodies." Science 344, no. 6184 (May 8, 2014): 588–89. http://dx.doi.org/10.1126/science.1254990.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Soelberg Sorensen, Per. "Review: Neutralizing antibodies against interferon-beta." Therapeutic Advances in Neurological Disorders 1, no. 2 (September 2008): 125–41. http://dx.doi.org/10.1177/1756285608095144.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Karuna, Shelly T., and Lawrence Corey. "Broadly Neutralizing Antibodies for HIV Prevention." Annual Review of Medicine 71, no. 1 (January 27, 2020): 329–46. http://dx.doi.org/10.1146/annurev-med-110118-045506.

Full text

Abstract:

In the last decade, over a dozen potent broadly neutralizing antibodies (bnAbs) to several HIV envelope protein epitopes have been identified, and their in vitro neutralization profiles have been defined. Many have demonstrated prevention efficacy in preclinical trials and favorable safety and pharmacokinetic profiles in early human clinical trials. The first human prevention efficacy trials using 10 sequential, every-two-month administrations of a single anti-HIV bnAb are anticipated to conclude in 2020. Combinations of complementary bnAbs and multi-specific bnAbs exhibit improved breadth and potency over most individual antibodies and are entering advanced clinical development. Genetic engineering of the Fc regions has markedly improved bnAb half-life, increased mucosal tissue concentrations of antibodies (especially in the genital tract), and enhanced immunomodulatory and Fc effector functionality, all of which improve antibodies' preventative and therapeutic potential. Human-derived monoclonal antibodies are likely to enter the realm of primary care prevention and therapy for viral infections in the near future.

APA, Harvard, Vancouver, ISO, and other styles

42

Julg, Boris, and Dan H. Barouch. "Neutralizing antibodies for HIV-1 prevention." Current Opinion in HIV and AIDS 14, no. 4 (July 2019): 318–24. http://dx.doi.org/10.1097/coh.0000000000000556.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Masuho, Y., Y. I. Matsumoto, T. Sugano, S. Fujinaga, and Y. Minamishima. "Human Monoclonal Antibodies Neutralizing Human Cytomegalovirus." Journal of General Virology 68, no. 5 (May 1, 1987): 1457–61. http://dx.doi.org/10.1099/0022-1317-68-5-1457.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Tong, Phuoc-Bao-Viet, Li-Yun Lin, and Tuan Hiep Tran. "Coronaviruses pandemics: Can neutralizing antibodies help?" Life Sciences 255 (August 2020): 117836. http://dx.doi.org/10.1016/j.lfs.2020.117836.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Opdenakker, Ghislain, Philippe E. Van den Steen, Geneviève Laureys, Kathleen Hunninck, and Bernd Arnold. "Neutralizing antibodies in gene-defective hosts." Trends in Immunology 24, no. 2 (February 2003): 94–100. http://dx.doi.org/10.1016/s1471-4906(02)00037-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Norley, S. G., and R. Kurth. "Neutralizing antibodies and antigens in AIDS." Infection 19, S2 (March 1991): S83—S88. http://dx.doi.org/10.1007/bf01644473.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Corti, Davide, Elisabetta Cameroni, Barbara Guarino, Nicole L. Kallewaard, Qing Zhu, and Antonio Lanzavecchia. "Tackling influenza with broadly neutralizing antibodies." Current Opinion in Virology 24 (June 2017): 60–69. http://dx.doi.org/10.1016/j.coviro.2017.03.002.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Laursen, Nick S., and Ian A. Wilson. "Broadly neutralizing antibodies against influenza viruses." Antiviral Research 98, no. 3 (June 2013): 476–83. http://dx.doi.org/10.1016/j.antiviral.2013.03.021.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Flemming, Alexandra. "Sequential vaccine elicits broadly neutralizing antibodies." Nature Reviews Drug Discovery 15, no. 11 (November 2016): 749. http://dx.doi.org/10.1038/nrd.2016.228.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Tikhonov, Ilia, Tracy J. Ruckwardt, Glen S. Hatfield, and C. David Pauza. "Tat-Neutralizing Antibodies in Vaccinated Macaques." Journal of Virology 77, no. 5 (March 1, 2003): 3157–66. http://dx.doi.org/10.1128/jvi.77.5.3157-3166.2003.

Full text

Abstract:

ABSTRACT The human immunodeficiency virus Tat protein is essential for virus replication and is a candidate vaccine antigen. Macaques immunized with Tat or chemically modified Tat toxoid having the same clade B sequence developed strong antibody responses. We compared these antisera for their abilities to recognize diverse Tat sequences. An overlapping peptide array covering three clade B and two clade C Tat sequences was constructed to help identify reactive linear epitopes. Sera from Tat-immunized macaques were broadly cross-reactive with clade B and clade C sequences but recognized a clade B-specific epitope in the basic domain. Sera from Tat toxoid-immunized macaques had a more restricted pattern of recognition, reacting mainly with clade B and with only one clade B basic domain sequence, which included the rare amino acids RPPQ at positions 57 to 60. Monoclonal antibodies against the amino terminus or the domain RPPQ sequence blocked Tat uptake into T cells and neutralized Tat in a cell-based transactivation assay. Macaques immunized with Tat or Tat toxoid proteins varied in their responses to minor epitopes, but all developed a strong response to the amino terminus, and antisera were capable of neutralizing Tat in a transactivation assay.

APA, Harvard, Vancouver, ISO, and other styles

Journal articles on the topic 'Neutralizing antibodies'

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles