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Journal articles on the topic 'Lipooligosaccharide'

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Published: 4 June 2021

Last updated: 20 February 2023

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1

Houliston, R. Scott, Evgeny Vinogradov, Monika Dzieciatkowska, Jianjun Li, Frank St. Michael, Marie-France Karwaski, Denis Brochu, et al. "Lipooligosaccharide ofCampylobacter jejuni." Journal of Biological Chemistry 286, no. 14 (January 21, 2011): 12361–70. http://dx.doi.org/10.1074/jbc.m110.181750.

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2

Sun, Shuhua, N. Karoline Scheffler, Bradford W. Gibson, Jing Wang, and Robert S. Munson. "Identification and Characterization of the N-Acetylglucosamine Glycosyltransferase Gene of Haemophilus ducreyi." Infection and Immunity 70, no. 10 (October 2002): 5887–92. http://dx.doi.org/10.1128/iai.70.10.5887-5892.2002.

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ABSTRACT Haemophilus ducreyi is the causative agent of chancroid, a sexually transmitted ulcerative disease. In the present study, the Neisseria gonorrhoeae lgtA lipooligosaccharide glycosyltransferase gene was used to identify a homologue in the genome of H. ducreyi. The putative H. ducreyi glycosyltransferase gene (designated lgtA) was cloned and insertionally inactivated, and an isogenic mutant was constructed. Structural studies demonstrated that the lipooligosaccharide isolated from the mutant strain lacked N-acetylglucosamine and distal sugars found in the lipooligosaccharide produced by the parental strain. The isogenic mutant was transformed with a recombinant plasmid containing the putative glycosyltransferase gene. This strain produced the lipooligosaccharide glycoforms produced by the parental strain, confirming that the lgtA gene encodes the N-acetylglucosamine glycosyltransferase.

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3

Pollard, Angela, Frank St. Michael, Lynn Connor, Wade Nichols, and Andrew Cox. "Structural characterization of Haemophilus parainfluenzae lipooligosaccharide and elucidation of its role in adherence using an outer core mutant." Canadian Journal of Microbiology 54, no. 11 (November 2008): 906–17. http://dx.doi.org/10.1139/w08-082.

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The opportunistic pathogen Haemophilus parainfluenzae is a gram-negative bacterium found in the oropharynx of humans. Haemophilus parainfluenzae is a member of the Pasteurellaceae family in which it is most closely related to Haemophilus sengis and Actinobacillus . Characterization of surface displayed lipooligosaccharide has identified components that are crucial in adherence. We examined the oligosaccharide structure of lipooligosaccharide from 2 clinical isolates of H. parainfluenzae. Core oligosaccharide was isolated by standard methods from purified lipooligosaccharide. Structural information was established by a combination of monosaccharide and methylation analyses, nuclear magnetic resonance spectroscopy, and mass spectrometry revealing the following structures: R-(1-6)-β-Glc-(1-4)-d,d-α-Hep-(1-6)-β-Glc-(1-4)- substituting a tri-heptose-Kdo inner core of L,d-α-Hep-(1-2)-l,d-α-Hep-(1-3)-l,d-α-Hep-(1-5)-α-Kdo at the 4-position of the proximal l,d-α-Hep residue to Kdo, and with a PEtn residue at the 6-position of the central l,d-α-Hep residue. In strain 4282, the R substituent is β-galactose and in strain 4201 there is no substituent at the distal glucose. These analyses have revealed that multiple structural aspects of H. parainfluenzae lipooligosaccharide are comparable with nontypeable Haemophilus influenzae lipooligosaccharide. This study also identified a galactan in strain 4201 and a glucan in strain 4282. Haemophilus parainfluenzae was shown to adhere to a bronchial epithelial cell line to the same degree as nontypeable H. influenzae. However, an H. parainfluenzae mutant lacking the outer core of the lipooligosaccharide showed diminished adherence to the epithelial cells, suggesting that H. parainfluenzae lipooligosaccharide plays a role in tissue colonization.

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Corsaro, M. Michela, Rosa Lanzetta, Ermenegilda Parrilli, Michelangelo Parrilli, M. Luisa Tutino, and Salvatore Ummarino. "Influence of Growth Temperature on Lipid and Phosphate Contents of Surface Polysaccharides from the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC 125." Journal of Bacteriology 186, no. 1 (January 1, 2004): 29–34. http://dx.doi.org/10.1128/jb.186.1.29-34.2004.

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ABSTRACT The chemical structural variations induced by different growth temperatures in the lipooligosaccharide and exopolysaccharide components extracted from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125 are described. The increase in phosphorylation with the increase in growth temperature seems to be general, because it happens not only for the lipooligosaccharide but also for the exopolysaccharide. Structural variations in the lipid components of lipid A also occur. In addition, free lipid A is found at both 25 and 4°C but not at 15°C, which is the optimal growth temperature, suggesting a incomplete biosynthesis of the lipooligosaccharide component under the first two temperature conditions.

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5

Greiner, L. L., H. Watanabe, N. J. Phillips, J. Shao, A. Morgan, A. Zaleski, B. W. Gibson, and M. A. Apicella. "Nontypeable Haemophilus influenzae Strain 2019 Produces a Biofilm Containing N-Acetylneuraminic Acid That May Mimic Sialylated O-Linked Glycans." Infection and Immunity 72, no. 7 (July 2004): 4249–60. http://dx.doi.org/10.1128/iai.72.7.4249-4260.2004.

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ABSTRACT Previous studies suggested that nontypeable Haemophilus influenzae (NTHI) can form biofilms during human and chinchilla middle ear infections. Microscopic analysis of a 5-day biofilm of NTHI strain 2019 grown in a continuous-flow chamber revealed that the biofilm had a diffuse matrix interlaced with multiple water channels. Our studies showed that biofilm production was significantly decreased when a chemically defined medium lacking N-acetylneuraminic acid (sialic acid) was used. Based on these observations, we examined mutations in seven NTHI strain 2019 genes involved in carbohydrate and lipooligosaccharide biosynthesis. NTHI strain 2019 with mutations in the genes encoding CMP-N-acetylneuraminic acid synthetase (siaB), one of the three NTHI sialyltransferases (siaA), and the undecaprenyl-phosphate α-N-acetylglucosaminyltransferase homolog (wecA) produced significantly smaller amounts of biofilm. NTHI strain 2019 with mutations in genes encoding phosphoglucomutase (pgm), UDP-galactose-4-epimerase, and two other NTHI sialyltransferases (lic3A and lsgB) produced biofilms that were equivalent to or larger than the biofilms produced by the parent strain. The biofilm formed by the NTHI strain 2019pgm mutant was studied with Maackia amurensis fluorescein isothiocyanate (FITC)-conjugated and Sambucus nigra tetramethyl rhodamine isocyanate (TRITC)-conjugated lectins. S. nigra TRITC-conjugated lectin bound to this biofilm, while M. amurensis FITC-conjugated lectin did not. S. nigra TRITC-conjugated lectin binding was inhibited by incubation with α2,6-neuraminyllactose and by pretreatment of the biofilm with Vibrio cholerae neuraminidase. Matrix-assisted laser desorption ionization—time of flight mass spectometry analysis of lipooligosaccharides isolated from a biofilm, the planktonic phase, and plate-grown organisms showed that the levels of most sialylated glycoforms were two- to fourfold greater when the lipooligosaccharide was derived from planktonic or biofilm organisms. Our data indicate that NTHI strain 2019 produces a biofilm containing α2,6-linked sialic acid and that the sialic acid content of the lipooligosaccharides increases concomitant with the transition of organisms to a biofilm form.

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6

Starner, Timothy D., W. Edward Swords, Michael A. Apicella, and Paul B. McCray. "Susceptibility of Nontypeable Haemophilus influenzae to Human β-Defensins Is Influenced by Lipooligosaccharide Acylation." Infection and Immunity 70, no. 9 (September 2002): 5287–89. http://dx.doi.org/10.1128/iai.70.9.5287-5289.2002.

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ABSTRACT Nontypeable Haemophilus influenzae (NTHI) lipooligosaccharide htrB mutants exhibited greater than 45-fold-increased sensitivity to human β-defensin 2 (HBD-2) compared to the wild type. Complementation by htrB in trans to acylation competence reversed this increased sensitivity. In contrast, NTHI was more susceptible to HBD-3 and showed no changes in sensitivity as a result of lipooligosaccharide mutations in oligosaccharide and lipid A biosynthesis genes.

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7

Lewis, Lisa A., Biswa Choudhury, Jacqueline T. Balthazar, Larry E. Martin, Sanjay Ram, Peter A. Rice, David S. Stephens, Russell Carlson, and William M. Shafer. "Phosphoethanolamine Substitution of Lipid A and Resistance of Neisseria gonorrhoeae to Cationic Antimicrobial Peptides and Complement-Mediated Killing by Normal Human Serum." Infection and Immunity 77, no. 3 (December 29, 2008): 1112–20. http://dx.doi.org/10.1128/iai.01280-08.

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ABSTRACT The capacity of Neisseria gonorrhoeae to cause disseminated gonococcal infection requires that such strains resist the bactericidal action of normal human serum. The bactericidal action of normal human serum against N. gonorrhoeae is mediated by the classical complement pathway through an antibody-dependent mechanism. The mechanism(s) by which certain strains of gonococci resist normal human serum is not fully understood, but alterations in lipooligosaccharide structure can affect such resistance. During an investigation of the biological significance of phosphoethanolamine extensions from lipooligosaccharide, we found that phosphoethanolamine substitutions from the heptose II group of the lipooligosaccharide β-chain did not impact levels of gonococcal (strain FA19) resistance to normal human serum or polymyxin B. However, loss of phosphoethanolamine substitution from the lipid A component of lipooligosaccharide, due to insertional inactivation of lptA, resulted in increased gonococcal susceptibility to polymyxin B, as reported previously for Neisseria meningitidis. In contrast to previous reports with N. meningitidis, loss of phosphoethanolamine attached to lipid A rendered strain FA19 susceptible to complement killing. Serum killing of the lptA mutant occurred through the classical complement pathway. Both serum and polymyxin B resistance as well as phosphoethanolamine decoration of lipid A were restored in the lptA-null mutant by complementation with wild-type lptA. Our results support a role for lipid A phosphoethanolamine substitutions in resistance of this strict human pathogen to innate host defenses.

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8

Grenier, Daniel. "Binding properties of Treponema denticola lipooligosaccharide." Journal of Oral Microbiology 5, no. 1 (January 1, 2013): 21517. http://dx.doi.org/10.3402/jom.v5i0.21517.

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9

Arking, Dan, Yanhong Tong, and Daniel C. Stein. "Analysis of Lipooligosaccharide Biosynthesis in theNeisseriaceae." Journal of Bacteriology 183, no. 3 (February 1, 2001): 934–41. http://dx.doi.org/10.1128/jb.183.3.934-941.2001.

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ABSTRACT Neisserial lipooligosaccharide (LOS) contains three oligosaccharide chains, termed the α, β, and γ chains. We used Southern hybridization experiments on DNA isolated from variousNeisseria spp. to determine if strains considered to be nonpathogenic possessed DNA sequences homologous with genes involved in the biosynthesis of these oligosaccharide chains. The presence or absence of specific genes was compared to the LOS profiles expressed by each strain, as characterized by their mobilities on sodium dodecyl sulfate-polyacrylamide gel electrophoresis gel and their reactivities with various LOS-specific monoclonal antibodies. A great deal of heterogeneity was seen with respect to the presence of genes encoding glycosyltransferases in Neisseria. All pathogenic species were found to possess DNA sequences homologous with the lgtgene cluster, a group of genes needed for the synthesis of the α chain. Some of these genes were also found to be present in strains considered to be nonpathogenic, such as Neisseria lactamica, N. subflava, and N. sicca. Some nonpathogenicNeisseria spp. were able to express high-molecular-mass LOS structures, even though they lacked the DNA sequences homologous withrfaF, a gene whose product must act before gonococcal and meningococcal LOS can be elongated. Using a PCR amplification strategy, in combination with DNA sequencing, we demonstrated that N. subflava 44 possessed lgtA, lgtB, andlgtE genes. The predicted amino acid sequence encoded by each of these genes suggested that they encoded functional proteins; however, structural analysis of LOS isolated from this strain indicated that the bulk of its LOS was not modified by these gene products. This suggests the existence of an additional regulatory mechanism that is responsible for the limited expression of these genes in this strain.

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10

Parker, Craig T., Michel Gilbert, Nobuhiro Yuki, Hubert P. Endtz, and Robert E. Mandrell. "Characterization of Lipooligosaccharide-Biosynthetic Loci of Campylobacter jejuni Reveals New Lipooligosaccharide Classes: Evidence of Mosaic Organizations." Journal of Bacteriology 190, no. 16 (June 13, 2008): 5681–89. http://dx.doi.org/10.1128/jb.00254-08.

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ABSTRACT The lipooligosaccharide (LOS) biosynthesis region is one of the more variable genomic regions between strains of Campylobacter jejuni. Indeed, eight classes of LOS biosynthesis loci have been established previously based on gene content and organization. In this study, we characterize additional classes of LOS biosynthesis loci and analyze various mechanisms that result in changes to LOS structures. To gain further insights into the genomic diversity of C. jejuni LOS biosynthesis region, we sequenced the LOS biosynthesis loci of 15 strains that possessed gene content that was distinct from the eight classes. This analysis identified 11 new classes of LOS loci that exhibited examples of deletions and insertions of genes and cassettes of genes found in other LOS classes or capsular biosynthesis loci leading to mosaic LOS loci. The sequence analysis also revealed both missense mutations leading to “allelic” glycosyltransferases and phase-variable and non-phase-variable gene inactivation by the deletion or insertion of bases. Specifically, we demonstrated that gene inactivation is an important mechanism for altering the LOS structures of strains possessing the same class of LOS biosynthesis locus. Together, these observations suggest that LOS biosynthesis region is a hotspot for genetic exchange and variability, often leading to changes in the LOS produced.

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11

Puig, Carmen, Sara Marti, Peter W. M. Hermans, Marien I. de Jonge, Carmen Ardanuy, Josefina Liñares, and Jeroen D. Langereis. "Incorporation of Phosphorylcholine into the Lipooligosaccharide of Nontypeable Haemophilus influenzae Does Not Correlate with the Level of Biofilm FormationIn Vitro." Infection and Immunity 82, no. 4 (January 22, 2014): 1591–99. http://dx.doi.org/10.1128/iai.01445-13.

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ABSTRACTNontypeableHaemophilus influenzae(NTHi) is an opportunistic pathogen that causes otitis media in children and community-acquired pneumonia or exacerbations of chronic obstructive pulmonary disease in adults. A large variety of studies suggest that biofilm formation by NTHi may be an important step in the pathogenesis of this bacterium. The objective of this report was to determine the relationship between the presence of phosphorylcholine in the lipooligosaccharide of NTHi and the level of biofilm formation. The study was performed on 111 NTHi clinical isolates collected from oropharyngeal samples of healthy children, middle ear fluid of children with otitis media, and sputum samples of patients with chronic obstructive pulmonary disease or community-acquired pneumonia. NTHi clinical isolates presented a large variation in the level of biofilm formation in a static assay and phosphorylcholine content. Isolates collected from the oropharynx and middle ear fluid of children tended to have more phosphorylcholine and made denser biofilms than isolates collected from sputum samples of patients with chronic obstructive pulmonary disease or community-acquired pneumonia. No correlation was observed between biofilm formation and the presence of phosphorylcholine in the lipooligosaccharide for either planktonic or biofilm growth. This lack of correlation was confirmed by abrogating phosphorylcholine incorporation into lipooligosaccharide throughlicAgene deletion, which had strain-specific effects on biofilm formation. Altogether, we present strong evidence to conclude that there is no correlation between biofilm formation in a static assay and the presence of phosphorylcholine in lipooligosaccharide in a large collection of clinical NTHi isolates collected from different groups of patients.

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12

Juneau, Richard A., Bing Pang, Kristin E. D. Weimer, Chelsie E. Armbruster, and W. Edward Swords. "NontypeableHaemophilus influenzaeInitiates Formation of Neutrophil Extracellular Traps." Infection and Immunity 79, no. 1 (October 18, 2010): 431–38. http://dx.doi.org/10.1128/iai.00660-10.

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ABSTRACTNontypeableHaemophilus influenzae(NTHI) is a leading cause of otitis media infections, which are often chronic and/or recurrent in nature. NTHI and other bacterial species persistin vivowithin biofilms during otitis media and other persistent infections. These biofilms have a significant host component that includes neutrophil extracellular traps (NETs). These NETs do not mediate clearance of NTHI, which survives within NET structures by means of specific subpopulations of lipooligosaccharides on the bacterial surface that are determinants of biofilm formationin vitro. In this study, the ability of NTHI and NTHI components to initiate NET formation was examined using anin vitromodel system. Both viable and nonviable NTHI strains were shown to promote NET formation, as did preparations of bacterial DNA, outer membrane proteins, and lipooligosaccharide (endotoxin). However, only endotoxin from a parental strain of NTHI exhibited equivalent potency in NET formation to that of NTHI. Additional studies showed that NTHI entrapped within NET structures is resistant to both extracellular killing within NETs and phagocytic killing by incoming neutrophils, due to oligosaccharide moieties within the lipooligosaccharides. Thus, we concluded that NTHI elicits NET formation by means of multiple pathogen-associated molecular patterns (most notably endotoxin) and is highly resistant to killing within NET structures. These data support the conclusion that, for NTHI, formation of NET structures may be a persistence determinant by providing a niche within the middle-ear chamber.

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13

Evans, J. S., and M. C. J. Maiden. "Purification of meningococcal lipooligosaccharide by FPLC techniques." Microbiology 142, no. 1 (January 1, 1996): 57–62. http://dx.doi.org/10.1099/13500872-142-1-57.

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14

Berrington, A. W., Y. C. Tan, Y. Srikhanta, B. Kuipers, P. Ley, I. R. A. Peak, and M. P. Jennings. "Phase variation in meningococcal lipooligosaccharide biosynthesis genes." FEMS Immunology & Medical Microbiology 34, no. 4 (December 2002): 267–75. http://dx.doi.org/10.1111/j.1574-695x.2002.tb00633.x.

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15

Nassif, Xavier. "Gonococcal lipooligosaccharide: an adhesin for bacterial dissemination?" Trends in Microbiology 8, no. 12 (December 2000): 539–40. http://dx.doi.org/10.1016/s0966-842x(00)01879-5.

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16

Gulati, Sunita, Sanjay Ram, Daniel P. McQuillen, Michael K. Pangburn, and Peter A. Rice. "Factor H interactions with sialylated gonococcal lipooligosaccharide." Molecular Immunology 35, no. 6-7 (April 1998): 398. http://dx.doi.org/10.1016/s0161-5890(98)90801-x.

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17

Syrogiannopoulos, G. A., E. J. Hansen, A. L. Erwin, R. S. Munford, J. Rutledge, J. S. Reisch, and G. H. McCracken. "Haemophilus influenzae Type b Lipooligosaccharide Induces Meningeal Inflammation." Journal of Infectious Diseases 157, no. 2 (February 1, 1988): 237–44. http://dx.doi.org/10.1093/infdis/157.2.237.

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18

Gaultier, Gabrielle N., Kayla N. Colledanchise, Alaa Alhazmi, and Marina Ulanova. "The Immunostimulatory Capacity of Nontypeable Haemophilus influenzae Lipooligosaccharide." Pathogens and Immunity 2, no. 1 (February 16, 2017): 34. http://dx.doi.org/10.20411/pai.v2i1.162.

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Background: We have recently found that lipooligosaccharide (LOS) isolated from encapsulated strains of Haemophilus influenzae (H. influenzae) has strong adjuvant, but diminished pro-inflammatory ability as compared to Escherichia coli lipopolysaccharide (LPS). In this study, we aimed to determine the immunostimulatory capacity of nontypeable/ non-encapsulated H. influenzae (NTHi) LOS by comparing the effect of killed bacteria with LOS isolated from the same strain.Methods: Following stimulation of human monocytic THP-1 cells with killed NTHi strain 375, or with the corresponding amount of LOS, we studied the protein and gene expression of immunostimulatory and antigen-presenting molecules, cytokines, and innate immune receptors.Results: Stimulation with LOS resulted in lower expression of adhesion (CD54, CD58) as well as costimulatory molecules (CD40, CD86), but in higher expression of antigen-presenting molecules (HLA-DR and HLA-ABC) compared to killed NTHi, whereas killed bacteria induced higher release of both TNF-α and IL-10. The results indicate that while LOS of NTHi has decreased capacity to induce pro-inflammatory responses compared to E. coli LPS or killed NTHi, this LOS has the potential to facilitate antigen presentation.Conclusions: Considering the important role of NTHi as a respiratory pathogen, and its currently increasing significance in the etiology of invasive infections, LOS deserves further attention as a vaccine antigen, which also has potent adjuvant properties.Keywords: Nontypeable Haemophilus influenzae, Lipooligosaccharide, THP-1 cells, innate immune responses

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19

HANSEN, ERIC J., GEORGE H. MCCRACKEN, and GEORGE SYROGIANNOPOULOS. "Haemophilus influenzae type b lipooligosaccharide induces meningeal inflammation." Pediatric Infectious Disease Journal 6, no. 12 (December 1987): 1150. http://dx.doi.org/10.1097/00006454-198706120-00027.

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20

HANSEN, ERIC J., GEORGE H. MCCRACKEN, and GEORGE SYROGIANNOPOULOS. "Haemophilus influenzae type b lipooligosaccharide induces meningeal inflammation." Pediatric Infectious Disease Journal 6, no. 12 (December 1987): 1150. http://dx.doi.org/10.1097/00006454-198712000-00027.

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21

Post, Deborah M. B., DeSheng Zhang, Jerrold P. Weiss, and Bradford W. Gibson. "Stable isotope metabolic labeling of Neisseria meningitidis lipooligosaccharide." Journal of Endotoxin Research 12, no. 2 (April 2006): 93–98. http://dx.doi.org/10.1177/09680519060120020501.

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22

Apicella, Michael A. "Gonococcal lipooligosaccharide: an adhesin for bacterial dissemination? Response." Trends in Microbiology 8, no. 12 (December 2000): 541. http://dx.doi.org/10.1016/s0966-842x(00)01880-1.

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23

Petricoin, E. F., and D. C. Stein. "Molecular analysis of lipooligosaccharide biosynthesis in Neisseria gonorrhoeae." Infection and Immunity 57, no. 9 (1989): 2847–52. http://dx.doi.org/10.1128/iai.57.9.2847-2852.1989.

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24

Danaher, R. J., J. C. Levin, D. Arking, C. L. Burch, R. Sandlin, and D. C. Stein. "Genetic basis of Neisseria gonorrhoeae lipooligosaccharide antigenic variation." Journal of bacteriology 177, no. 24 (1995): 7275–79. http://dx.doi.org/10.1128/jb.177.24.7275-7279.1995.

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25

Alibaud, Laeticia, Jakub Pawelczyk, Laila Gannoun-Zaki, Vipul K. Singh, Yoann Rombouts, Michel Drancourt, Jaroslaw Dziadek, Yann Guérardel, and Laurent Kremer. "Increased Phagocytosis ofMycobacterium marinumMutants Defective in Lipooligosaccharide Production." Journal of Biological Chemistry 289, no. 1 (November 14, 2013): 215–28. http://dx.doi.org/10.1074/jbc.m113.525550.

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26

Kerwood, Deborah E., Herman Schneider, and Ryohei Yamasaki. "Structural analysis of lipooligosaccharide produced by Neisseria gonorrhoeae, strain MS11mk (variant A): a precursor for a gonococcal lipooligosaccharide associated with virulence." Biochemistry 31, no. 51 (December 1992): 12760–68. http://dx.doi.org/10.1021/bi00166a008.

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27

Estabrook, M. M., R. E. Mandrell, M. A. Apicella, and J. M. Griffiss. "Measurement of the human immune response to meningococcal lipooligosaccharide antigens by using serum to inhibit monoclonal antibody binding to purified lipooligosaccharide." Infection and Immunity 58, no. 7 (1990): 2204–13. http://dx.doi.org/10.1128/iai.58.7.2204-2213.1990.

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28

Jones, Allison, Miriam Geörg, Lisa Maudsdotter, and Ann-Beth Jonsson. "Endotoxin, Capsule, and Bacterial Attachment Contribute to Neisseria meningitidis Resistance to the Human Antimicrobial Peptide LL-37." Journal of Bacteriology 191, no. 12 (April 17, 2009): 3861–68. http://dx.doi.org/10.1128/jb.01313-08.

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ABSTRACT Pathogenic bacteria have evolved numerous mechanisms to evade the human immune system and have developed widespread resistance to traditional antibiotics. We studied the human pathogen Neisseria meningitidis and present evidence of novel mechanisms of resistance to the human antimicrobial peptide LL-37. We found that bacteria attached to host epithelial cells are resistant to 10 μM LL-37 whereas bacteria in solution or attached to plastic are killed, indicating that the cell microenvironment protects bacteria. The bacterial endotoxin lipooligosaccharide and the polysaccharide capsule contribute to LL-37 resistance, probably by preventing LL-37 from reaching the bacterial membrane, as more LL-37 reaches the bacterial membrane on both lipooligosaccharide-deficient and capsule-deficient mutants whereas both mutants are also more susceptible to LL-37 killing than the wild-type strain. N. meningitidis bacteria respond to sublethal doses of LL-37 and upregulate two of their capsule genes, siaC and siaD, which further results in upregulation of capsule biosynthesis.

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29

Marsden, Gemma L., Jianjun Li, Paul H. Everest, Andrew J. Lawson, and Julian M. Ketley. "Creation of a Large Deletion Mutant of Campylobacter jejuni Reveals that the Lipooligosaccharide Gene Cluster Is Not Required for Viability." Journal of Bacteriology 191, no. 7 (January 30, 2009): 2392–99. http://dx.doi.org/10.1128/jb.01397-08.

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ABSTRACT Deletion of the lipooligosaccharide biosynthesis region (Cj1132c to Cj1152c) from the genome of Campylobacter jejuni NCTC11168 shows that the core is not required for viability. The mutant was attenuated for growth and has increased sensitivity to antibiotics and detergents. Natural transformation and invasion of cultured host cells was abolished.

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30

Choi, Joshua, Andrew D. Cox, Jianjun Li, William McCready, and Marina Ulanova. "Activation of Innate Immune Responses by Haemophilus influenzae Lipooligosaccharide." Clinical and Vaccine Immunology 21, no. 5 (March 26, 2014): 769–76. http://dx.doi.org/10.1128/cvi.00063-14.

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ABSTRACTA Gram-negative pathogenHaemophilus influenzaehas a truncated endotoxin known as lipooligosaccharide (LOS). Recent studies onH. influenzaeLOS highlighted its structural and compositional implications for bacterial virulence; however, the role of LOS in the activation of innate and adaptive immunity is poorly understood. THP-1 monocytes were stimulated with either lipopolysaccharide (LPS) fromEscherichia colior LOS compounds derived fromH. influenzaeEagan, Rd, and Rdlic1 lpsAstrains. Cell surface expression of key antigen-presenting, costimulatory, and adhesion molecules, as well as gene expression of some cytokines and pattern recognition receptors, were studied. Eagan and Rd LOS had a lower capacity to induce the expression of ICAM-1, CD40, CD58, tumor necrosis factor alpha (TNF-α), and interleukin-1β (IL-1β) compared to LPS. In contrast, antigen-presenting (HLA-ABC or HLA-DR) and costimulatory (CD86) molecules and NOD2 were similarly upregulated in response to LOS and LPS. LOS from a mutant Rd strain (Rdlic1 lpsA) consistently induced higher expression of innate immune molecules than the wild-type LOS, suggesting the importance of phosphorylcholine and/or oligosaccharide extension in cellular responses to LOS. An LOS compound with a strong ability to upregulate antigen-presenting and costimulatory molecules combined with a low proinflammatory activity may be considered a vaccine candidate to immunize againstH. influenzae.

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31

Albiger, Barbara, Linda Johansson, and Ann-Beth Jonsson. "Lipooligosaccharide-Deficient Neisseria meningitidis Shows Altered Pilus-Associated Characteristics." Infection and Immunity 71, no. 1 (January 2003): 155–62. http://dx.doi.org/10.1128/iai.71.1.155-162.2003.

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ABSTRACT Molecular interaction between host mucosal surfaces and outer membrane components of microbes is crucial in the infection process. The outer membrane of pathogenic Neisseria contains surface molecules such as pili, PilC, and Opa and a monolayer of lipooligosaccharide (LOS), all of which are involved in the interaction with host cells. Pili mediate the initial attachment to human epithelial cells, which is followed by tight contact between bacteria and the eucaryotic cells, leading to bacterial invasion. To further examine the basis for bacterium-host cell contact, we constructed an LOS-deficient Neisseria meningitidis serogroup C mutant. LOS deficiency was without exception accompanied by altered colony opacity and morphology, which most likely represented an “on” switch for Opa540 expression, and by reduced levels of the iron-regulated proteins FetA and FbpA. We show here that LOS is essential for pilus-associated adherence but dispensable for fiber formation and twitching motility. The absence of attachment to epithelial cells could not be attributed to altered levels of piliation or defects in the pilus adhesion phenotype. Further, LOS mutants do not invade host cells and have lost the natural competence for genetic transformation.

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32

Marr, Nico, Alexey Novikov, Adeline M. Hajjar, Martine Caroff, and Rachel C. Fernandez. "Variability in the Lipooligosaccharide Structure and Endotoxicity amongBordetella pertussisStrains." Journal of Infectious Diseases 202, no. 12 (December 15, 2010): 1897–906. http://dx.doi.org/10.1086/657409.

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33

McLaughlin, R., S. M. Spinola, and M. A. Apicella. "Generation of lipooligosaccharide mutants of Haemophilus influenzae type b." Journal of Bacteriology 174, no. 20 (1992): 6455–59. http://dx.doi.org/10.1128/jb.174.20.6455-6459.1992.

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34

Sandlin, R. C., and D. C. Stein. "Role of phosphoglucomutase in lipooligosaccharide biosynthesis in Neisseria gonorrhoeae." Journal of Bacteriology 176, no. 10 (1994): 2930–37. http://dx.doi.org/10.1128/jb.176.10.2930-2937.1994.

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35

PHONGSISAY, V., and B. FRY. "Bidirectional transcription of lipooligosaccharide synthesis genes from Campylobacter jejuni." International Journal of Medical Microbiology 297, no. 6 (October 15, 2007): 431–41. http://dx.doi.org/10.1016/j.ijmm.2007.05.003.

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36

Ahmed, H. J., S. Borrelli, J. Jonasson, L. Eriksson, S. Hanson, B. Höjer, M. Sunkuntu, et al. "Monoclonal antibodies againstHaemophilus ducreyi lipooligosaccharide and their diagnostic usefulness." European Journal of Clinical Microbiology & Infectious Diseases 14, no. 10 (October 1995): 892–98. http://dx.doi.org/10.1007/bf01691496.

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37

Ram, Sanjay, Andrew D. Cox, J. Claire Wright, Ulrich Vogel, Silke Getzlaff, Ryan Boden, Jianjun Li, et al. "Neisserial Lipooligosaccharide Is a Target for Complement Component C4b." Journal of Biological Chemistry 278, no. 51 (October 2, 2003): 50853–62. http://dx.doi.org/10.1074/jbc.m308364200.

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38

Lin, Leo Y. C., Bojana Rakic, Cecilia P. C. Chiu, Emilie Lameignere, Warren W. Wakarchuk, Stephen G. Withers, and Natalie C. J. Strynadka. "Structure and Mechanism of the Lipooligosaccharide Sialyltransferase fromNeisseria meningitidis." Journal of Biological Chemistry 286, no. 43 (August 31, 2011): 37237–48. http://dx.doi.org/10.1074/jbc.m111.249920.

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39

Giles, Sarah K., Uwe H. Stroeher, Bhavya Papudeshi, Robert A. Edwards, Jessica AP Carlson-Jones, Michael Roach, and Melissa H. Brown. "The StkSR Two-Component System Influences Colistin Resistance in Acinetobacter baumannii." Microorganisms 10, no. 5 (May 8, 2022): 985. http://dx.doi.org/10.3390/microorganisms10050985.

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Acinetobacter baumannii is an opportunistic human pathogen responsible for numerous severe nosocomial infections. Genome analysis on the A. baumannii clinical isolate 04117201 revealed the presence of 13 two-component signal transduction systems (TCS). Of these, we examined the putative TCS named here as StkSR. The stkR response regulator was deleted via homologous recombination and its progeny, ΔstkR, was phenotypically characterized. Antibiogram analyses of ΔstkR cells revealed a two-fold increase in resistance to the clinically relevant polymyxins, colistin and polymyxin B, compared to wildtype. PAGE-separation of silver stained purified lipooligosaccharide isolated from ΔstkR and wildtype cells ruled out the complete loss of lipooligosaccharide as the mechanism of colistin resistance identified for ΔstkR. Hydrophobicity analysis identified a phenotypical change of the bacterial cells when exposed to colistin. Transcriptional profiling revealed a significant up-regulation of the pmrCAB operon in ΔstkR compared to the parent, associating these two TCS and colistin resistance. These results reveal that there are multiple levels of regulation affecting colistin resistance; the suggested ‘cross-talk’ between the StkSR and PmrAB two-component systems highlights the complexity of these systems.

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Blake, M. S., C. M. Blake, M. A. Apicella, and R. E. Mandrell. "Gonococcal opacity: lectin-like interactions between Opa proteins and lipooligosaccharide." Infection and immunity 63, no. 4 (1995): 1434–39. http://dx.doi.org/10.1128/iai.63.4.1434-1439.1995.

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41

Pettit, R. K., E. S. Martin, S. M. Wagner, and V. J. Bertolino. "Phenotypic modulation of gonococcal lipooligosaccharide in acidic and alkaline culture." Infection and immunity 63, no. 7 (1995): 2773–75. http://dx.doi.org/10.1128/iai.63.7.2773-2775.1995.

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42

Inzana, T. J., J. Hensley, J. McQuiston, A. J. Lesse, A. A. Campagnari, S. M. Boyle, and M. A. Apicella. "Phase variation and conservation of lipooligosaccharide epitopes in Haemophilus somnus." Infection and immunity 65, no. 11 (1997): 4675–81. http://dx.doi.org/10.1128/iai.65.11.4675-4681.1997.

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43

Tong, Y., D. Arking, S. Ye, B. Reinhold, V. Reinhold, and D. C. Stein. "Neisseria gonorrhoeaestrain PID2 simultaneously expresses six chemically related lipooligosaccharide structures." Glycobiology 12, no. 9 (September 1, 2002): 523–33. http://dx.doi.org/10.1093/glycob/cwf047.

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44

Silipo, Alba, Antonio Molinaro, Luisa Sturiale, J. Maxwell Dow, Gitte Erbs, Rosa Lanzetta, Mari-Anne Newman, and Michelangelo Parrilli. "The Elicitation of Plant Innate Immunity by Lipooligosaccharide ofXanthomonas campestris." Journal of Biological Chemistry 280, no. 39 (July 27, 2005): 33660–68. http://dx.doi.org/10.1074/jbc.m506254200.

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45

Ren, Huiping, Lynn G. Dover, Salim T. Islam, David C. Alexander, Jeffrey M. Chen, Gurdyal S. Besra, and Jun Liu. "Identification of the lipooligosaccharide biosynthetic gene cluster from Mycobacterium marinum." Molecular Microbiology 63, no. 5 (March 2007): 1345–59. http://dx.doi.org/10.1111/j.1365-2958.2007.05603.x.

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46

Inzana, Thomas J., Jennifer Hensley, John McQuiston, Alan J. Lesse, Anthony A. Campagnari, Stephen M. Boyle, and Michael A. Apicella. "Phase Variation and Conservation of Lipooligosaccharide Epitopes in Haemophilus somnus." Infection and Immunity 66, no. 8 (August 1, 1998): 4010. http://dx.doi.org/10.1128/iai.66.8.4010-4010.1998.

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Mertsola, J., R. S. Munford, O. Ramilo, X. Sáez-Llorens, M. M. Mustafa, G. H. McCracken, and E. J. Hansen. "Specific detection of Haemophilus influenzae type b lipooligosaccharide by immunoassay." Journal of Clinical Microbiology 28, no. 12 (1990): 2700–2706. http://dx.doi.org/10.1128/jcm.28.12.2700-2706.1990.

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Lewis, Lisa, Sanjay Ram, Jacqueline Balthazar, Larry Martin, Yih-Ling Tzeng, David Stephens, Peter Rice, and William Shafer. "Gonococcal lipooligosaccharide phosphoethanolamine substitutions modulate serum resistance and C4bp binding." Molecular Immunology 44, no. 1-3 (January 2007): 204–5. http://dx.doi.org/10.1016/j.molimm.2006.07.135.

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49

Arya, Subhash C. "Serological diagnosis of tuberculosis employing lipooligosaccharide antigen in developing countries." Tubercle and Lung Disease 77, no. 3 (June 1996): 291. http://dx.doi.org/10.1016/s0962-8479(96)90017-9.

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50

Campagnari, Anthony A., Stanley M. Spinola, Alan J. Lesse, Yousef Abu Kwaik, Robert E. Mandrell, and Michael A. Apicella. "Lipooligosaccharide epitopes shared among Gram-negative non-enteric mucosal pathogens." Microbial Pathogenesis 8, no. 5 (May 1990): 353–62. http://dx.doi.org/10.1016/0882-4010(90)90094-7.

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