Biological activities of a synthetic peptide composed of two unlinked domains from a retroviral transmembrane protein sequence.

Abstract:

:We report several biological activities of a synthetic peptide whose sequence contains the highly conserved region of feline leukemia virus transmembrane protein (TM) synthetically linked to another short TM-derived sequence particularly rich in polar positive residues. This 29-amino-acid peptide blocked [3H]thymidine uptake 30 to 50% by concanavalin A-stimulated CD4(+)--but not CD8(+)-enriched murine splenocytes. Maximal suppression was detected at 12.5 micrograms (3 microM) to 75 micrograms (19 microM) per ml of growth medium; stimulation of [3H]thymidine uptake was observed at higher peptide concentrations. The synthetic peptide inhibited but did not stimulate [3H]thymidine uptake by mitogen-activated thymocytes and antibody production by splenocytes as determined in a liquid hemolytic plaque assay. Similarities are reported between a consensus sequence of diverse retroviral TMs and a region of alpha interferons shown by others to be important for antiviral and cytostatic properties. The TM sequence-derived synthetic peptide blocked in a nontoxic and sequence-specific manner the release of murine leukemia virus from two chronically infected cell lines. We suggest that some of the biological effects of retroviral TM are mediated through a common pathway shared with alpha interferons.

journal_name

J Virol

journal_title

Journal of virology

authors

Wegemer DE,Kabat KG,Kloetzer WS

doi

10.1128/JVI.64.4.1429-1436.1990

subject

Has Abstract

pub_date

1990-04-01 00:00:00

pages

1429-36

issue

4

eissn

0022-538X

issn

1098-5514

journal_volume

64

pub_type

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