Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Variable Loop Glycan Dependency of the Broad and Potent HIV-1-Neutralizing Antibodies PG9 and PG16

5 Aug 2010

Abstract excerpt

The HIV-1-specific antibodies PG9 and PG16 show marked cross-isolate neutralization breadth and potency. Antibody neutralization has been shown to be dependent on the presence of N-linked glycosylation at position 160 in gp120. We show here that (i) the loss of several key glycosylation sites in the V1, V2, and V3 loops; (ii) the generation of pseudoviruses in the presence of various glycosidase inhibitors; and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Glycosylation and Glycoproteins Research
Share to HIV Research and Treatment
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20686044
DOI: 10.1128/jvi.00552-10

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Variable Loop Glycan Dependency of the Broad and Potent HIV-1-Neutralizing Antibodies PG9 and PG16PMID 20686044Read ↗

Crystal Structure of PG16 and Chimeric Dissection with Somatically Related PG9: Structure-Function Analysis of Two Quaternary-Specific Antibodies That Effectively Neutralize HIV-1Semantic proximity Read ↗

Subtle alteration of residues including N-linked glycans in V2 loop modulate HIV-1 neutralization by PG9 and PG16 monoclonal antibodiesSemantic proximity Read ↗

A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield.Semantic proximity Read ↗

N463 Glycosylation Site on V5 Loop of a Mutant gp120 Regulates the Sensitivity of HIV-1 to Neutralizing Monoclonal Antibodies VRC01/03.Semantic proximity Read ↗

A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralizationSemantic proximity Read ↗

Glycan-Dependent Neutralizing Antibodies Are Frequently Elicited in Individuals Chronically Infected with HIV-1 Clade B or C.Semantic proximity Read ↗

Mechanisms of escape from the PGT128 family of anti-HIV broadly neutralizing antibodies.Semantic proximity Read ↗

The C108g epitope in the V2 domain of gp120 functions as a potent neutralization target when introduced into envelope proteins derived from human immunodeficiency virus type 1 primary isolates.Semantic proximity Read ↗

A Short Segment of the HIV-1 gp120 V1/V2 Region Is a Major Determinant of Resistance to V1/V2 Neutralizing AntibodiesSemantic proximity Read ↗

Identification of an HIV-1 clade A envelope that exhibits broad antigenicity and neutralization sensitivity and elicits antibodies targeting three distinct epitopes.Semantic proximity Read ↗

A Limited Number of Antibody Specificities Mediate Broad and Potent Serum Neutralization in Selected HIV-1 Infected IndividualsSemantic proximity Read ↗

Effects of mutations on HIV-1 infectivity and neutralization involving the conserved NNNT amino acid sequence in the gp120 V3 loop.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.