About: Cross-Reactive Human IgM-Derived Monoclonal Antibodies that Bind to HIV-1 Envelope Glycoproteins

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Cross-Reactive Human IgM-Derived Monoclonal Antibodies that Bind to HIV-1 Envelope Glycoproteins Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Cross-Reactive Human IgM-Derived Monoclonal Antibodies that Bind to HIV-1 Envelope Glycoproteins
Creator	Zhu, Zhongyu Chen, Weizao Liao, Huaxin Broder, Christopher Dimitrov, Dimiter Haynes, Barton Quinnan, Gerald
source	Medline; PMC
abstract	Elicitation of antibodies with potent and broad neutralizing activity against HIV by immunization remains a challenge. Several monoclonal antibodies (mAbs) isolated from humans with HIV-1 infection exhibit such activity but vaccine immunogens based on structures containing their epitopes have not been successful for their elicitation. All known broadly neutralizing mAbs (bnmAbs) are immunoglobulin (Ig) Gs (IgGs) and highly somatically hypermutated which could impede their elicitation. Ig Ms (IgMs) are on average significantly less divergent from germline antibodies and are relevant for the development of vaccine immunogens but are underexplored compared to IgGs. Here we describe the identification and characterization of several human IgM-derived mAbs against HIV-1 which were selected from a large phage-displayed naive human antibody library constructed from blood, lymph nodes and spleens of 59 healthy donors. These antibodies bound with high affinity to recombinant envelope glycoproteins (gp140s, Envs) of HIV-1 isolates from different clades. They enhanced or did not neutralize infection by some of the HIV-1 primary isolates using CCR5 as a coreceptor but neutralized all CXCR4 isolates tested although weakly. One of these antibodies with relatively low degree of somatic hypermutation was more extensively characterized. It bound to a highly conserved region partially overlapping with the coreceptor binding site and close to but not overlapping with the CD4 binding site. These results suggest the existence of conserved structures that could direct the immune response to non-neutralizing or even enhancing antibodies which may represent a strategy used by the virus to escape neutralizing immune responses. Further studies will show whether such a strategy plays a role in HIV infection of humans, how important that role could be, and what the mechanisms of infection enhancement are. The newly identified mAbs could be used as reagents to further characterize conserved non-neutralizing, weakly neutralizing or enhancing epitopes and modify or remove them from candidate vaccine immunogens.
has issue date	2010-02-04(xsd:dateTime)
bibo:doi	10.3390/v2020547
bibo:pmid	21755021
has license	cc-by
sha1sum (hex)	b470eec84fd5bb0a9a7079506df05c3cdf398832
schema:url	https://doi.org/10.3390/v2020547
resource representing a document's title	Cross-Reactive Human IgM-Derived Monoclonal Antibodies that Bind to HIV-1 Envelope Glycoproteins
has PubMed Central identifier	PMC3133461
has PubMed identifier	21755021
schema:publication	Viruses
resource representing a document's body	covid:b470eec84fd5bb0a9a7079506df05c3cdf398832#body_text
is schema:about of	named entity 'based' named entity 'antibody' named entity 'neutralized' named entity 'human' named entity 'recombinant' named entity 'mAbs' named entity 'vaccine' named entity 'IgMs' named entity 'ENVELOPE' named entity 'HIV-1' named entity 'DIFFERENT' named entity 'BROAD' named entity 'BOUND' named entity 'CHALLENGE' named entity 'DISPLAYED' named entity 'LARGE' named entity 'MONOCLONAL ANTIBODIES' named entity 'DIVERGENT FROM' named entity 'PHAGE' named entity 'HIGH' named entity 'IMMUNOGENS' named entity 'AFFINITY' named entity 'DONORS' covid:arg/b470eec84fd5bb0a9a7079506df05c3cdf398832 named entity 'HERE' named entity 'CONSERVED REGION' named entity 'STRUCTURES' named entity 'GLYCOPROTEINS' named entity 'TESTED' named entity 'GERMLINE' named entity 'DERIVED' named entity 'CHARACTERIZED' named entity 'ENHANCED' named entity 'HIV-1' named entity 'LYMPH NODES' named entity 'THESE' named entity 'HUMAN IGM' named entity 'GLYCOPROTEINS' named entity 'DERIVED' named entity 'HIV' named entity 'HUMANS' named entity 'ONE OF' named entity 'SOMATIC HYPERMUTATION' named entity 'USING' named entity 'CORECEPTOR' named entity 'LOW' named entity 'SUCCESSFUL' named entity 'IDENTIFICATION' named entity 'RELEVANT' named entity 'VACCINE' named entity 'HUMAN' named entity 'CXCR4' named entity 'HUMAN IGM' named entity 'PRIMARY' named entity 'DEVELOPMENT' named entity 'ANTIBODIES' named entity 'RECOMBINANT' named entity 'DEGREE' named entity 'THEIR' named entity 'HEALTHY' named entity 'INFECTION' named entity 'ACTIVITY' named entity 'BASED' named entity 'SELECTED' named entity 'CCR5' named entity 'BLOOD' named entity 'IMMUNIZATION' named entity 'COMPARED' named entity 'EXHIBIT' named entity 'CROSS-REACTIVE' named entity 'SPLEENS' named entity 'ANTIBODY LIBRARY' named entity 'HIV-1 INFECTION' named entity 'BUT' named entity 'ISOLATED'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software