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Article

Role of the V2, V3, and CD4-binding domains of GP120 in curdlan sulfate neutralization sensitivity of HIV-1 during infection of T lymphocytes.

Virology - 15 Dec 1996

Jagodzinski P P, Wustner J, Kmieciak D, Wasik T J, Fertala A, Sieron A L, Takahashi M, Tsuji T, Mimura T, Fung M S, Gorny M K, Kloczewiak M, Kaneko Y, Kozbor D

Abstract excerpt

A sulfated polysaccharide, curdlan sulfate (CRDS) with 1,3-beta-D-glucan as a main chain, inhibits HIV-1 infection of human peripheral blood lymphocytes (PBLs) by binding to the V3 region of gp 120. We previously showed that T cell (T)-tropic HIV-1 isolates are over 10-fold more sensitive to neutralization by CRDS than macrophage (MT)-tropic viruses, which possesses a relatively less charged amino acid...

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Identifiers

PMID: 8955041
DOI: 10.1006/viro.1996.0649

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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