CD4 receptor binding peptides that block HIV infectivity cause human monocyte chemotaxis. Relationship to vasoactive intestinal polypeptide.

Abstract:

:The octapeptide Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr (peptide T) and two structural analogs are potent agonists of human monocyte chemotaxis, evincing identical rank potency orders as was previously shown for their inhibition of human immunodeficiency virus (HIV) envelope binding and T cell infectivity. Chemotactic activity could be inhibited by anti-CD4 monoclonal antibodies (Mabs), but not other mononuclear cell Mabs. The core peptide required for chemotactic activity is a pentapeptide related to the sequence Thr-Thr-Asn-Tyr-Thr. Homologous pentapeptides, identified by computer search, were detected in several other non-HIV-related viruses as well as the neuropeptide vasoactive intestinal polypeptide (VIP). The CD4 molecule, therefore, appears to be a recognition molecule for a small signal peptide ligand whose active sequence is a homolog of peptide T and which may be the neuropeptide VIP.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ruff MR,Martin BM,Ginns EI,Farrar WL,Pert CB

doi

10.1016/0014-5793(87)81265-6

subject

Has Abstract

pub_date

1987-01-19 00:00:00

pages

17-22

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(87)81265-6

journal_volume

211

pub_type

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