Leucine zipper domain of HIV-1 gp41 interacted specifically with alpha-catenin.

Abstract:

:Interactions between viral and cellular proteins could explain the molecular mechanisms behind the viral life cycle of HIV-1. The envelope protein gp41 of HIV-1 specifically interacted with alpha-catenin, not with beta-catenin. This interaction was shown by in vitro protein assay and in vivo transfected cell systems. Microinjection of the DNA expressing HIV-1 gp160 and alpha-catenin, into the HeLa cell, resulted in the colocalization of gp41 and alpha-catenin. Interestingly the noncleavable mutant of gp160 and alpha-catenin were found to be colocalized in the cell membrane. Mapping of the interaction sites between these two proteins revealed that the leucine zipper-like structure, located between the first and second alpha-helix domains from the carboxy terminus of HIV-1 gp41, interacted strongly with the carboxy terminus of alpha-catenin.

authors

Kim JT,Kim EM,Lee KH,Choi JE,Jhun BH,Kim JW

doi

10.1006/bbrc.2002.6583

subject

Has Abstract

pub_date

2002-03-15 00:00:00

pages

1239-44

issue

5

eissn

0006-291X

issn

1090-2104

pii

S0006291X02965836

journal_volume

291

pub_type

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