Groove-type Recognition of Chlamydiaceae-specific Lipopolysaccharide Antigen by a Family of Antibodies Possessing an Unusual Variable Heavy Chain N-Linked Glycan

Haji-Ghassemi, O.; Müller‐Loennies, Sven; Saldova, Radka; Muniyappa, Mohankumar; Brade, Lore; Rudd, Pauline M.; Harvey, David J.; Kosma, Paul; Brade, Helmut; Evans, Stephen V.

doi:10.1074/jbc.m113.528224

Cited by 16 publications

(33 citation statements)

References 74 publications

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“…Thus, the enveloping capacity of antibody binding sites can allow for very specific recognition. 51,52 A range of experimental techniques, including synthetic chemistry, antibody engineering, microarray technology and NMR, alongside computational approaches have been key to elucidate molecular structural features that modulate glycan-antibody recognition. [53][54][55][56][57] In this regard, antibody engineering and molecular modelling have been applied to demonstrate that in both pyranoside-and furanoside-antibody systems, the affinity and specificity mostly rely on CH-p interactions.…”

Section: Figmentioning

confidence: 99%

The challenges of glycan recognition with natural and artificial receptors

et al. 2019

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Section: Figmentioning

confidence: 99%

The challenges of glycan recognition with natural and artificial receptors

et al. 2019

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“…The common feature of the three HIV bnAb classes described is that the weak protein-carbohydrate interactions are overcome through multivalent binding to multiple glycans and protein residues within one Fab. Interestingly, crystal structures of Abs binding to other glycan antigens show whole saccharide units binding either within a pocket or groove [51, 52]. However, the majority of HIV glycan-binding bnAbs, with the exception of 2G12, bind across the face of the glycan [53].…”

Section: Hiv-1 Bnabs Target Envelope Glycansmentioning

confidence: 99%

Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design

Crispin

Doores

2015

Current Opinion in Virology

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The surface of enveloped viruses can be extensively glycosylated. Unlike the glycans coating pathogens such as bacteria and fungi, glycans on viruses are added and processed by the host-cell during biosynthesis. Glycoproteins are typically subjected to α-mannosidase processing and Golgi-mediated glycosyltransferase extension to form complex-type glycans. In envelope viruses, exceptions to this default pathway are common and lead to the presence of oligomannose-type glycan structures on the virion surface. In one extreme example, HIV-1 utilizes a high density of glycans to limit host antibody recognition of protein. However, the high density limits glycan processing and the resulting oligomannose structures can be recognised by broadly neutralising antibodies isolated form HIV-1 infected patients. Here we discuss how divergence from host-cell glycosylation can be targeted for vaccine design.

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“…Early studies showed that even highly specific induced IgM and IgG monoclonal antibodies used for cell typing (anti‐HLA, anti‐H2 and anti‐blood group antigens) were autopolyreactive . It was also established that almost all autopolyreactive NAAbs recognized conformational epitopes . Taking into consideration the above observations, the autopolyreactivity, as revealed by these techniques, could be related to the presence of various active binding sites situated in different spatial locations on the paratopes of antibodies that probably take part in the recognition of three dimensional structures.…”

Section: Humoral and Cellular Features Of Naabsmentioning

confidence: 99%

Autopolyreactivity Confers a Holistic Role in the Immune System

Avraméas

2016

Scand J Immunol

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In this review, we summarize and discuss some key findings from the study of naturally occurring autoantibodies. The B-cell compartment of the immune system appears to recognize almost all endogenous and environmental antigens. This ability is accomplished principally through autopolyreactive humoral and cellular immune receptors. This extended autopolyreactivity (1) along immunoglobulin gene recombination contributes to the immune system's ability to recognize a very large number of self and non-self constituents; and (2) generates a vast immune network that creates communication channels between the organism's interior and exterior. Thus, the immune system continuously evolves depending on the internal and external stimuli it encounters. Furthermore, this far-reaching network's existence implies activities resembling those of classical biological factors or activities that modulate the function of other classical biological factors. A few such antibodies have already been found. Another important concept is that natural autoantibodies are highly dependent on the presence or absence of commensal microbes in the organism. These results are in line with past and recent findings showing the fundamental influence of the microbiota on proper immune system development, and necessitate the existence of a host-microbe homeostasis. This homeostasis requires that the participating humoral and cellular receptors are able to recognize self-antigens and commensal microbes without damaging them. Autopolyreactive immune receptors expressing low affinity for both types of antigens fulfil this role. The immune system appears to play a holistic role similar to that of the nervous system.

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Groove-type Recognition of Chlamydiaceae-specific Lipopolysaccharide Antigen by a Family of Antibodies Possessing an Unusual Variable Heavy Chain N-Linked Glycan

Cited by 16 publications

References 74 publications

The challenges of glycan recognition with natural and artificial receptors

The challenges of glycan recognition with natural and artificial receptors

Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design

Autopolyreactivity Confers a Holistic Role in the Immune System

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