Shared motifs of the capsid proteins of hepadnaviruses and retroviruses suggest a common evolutionary origin.

Abstract:

:The structure of the dimeric C-terminal domain of the HIV-1 capsid protein (CA), recently determined by X-ray crystallography (Gamble et al. (1997)), has a notable resemblance to the structure of the hepatitis B virus (HBV) capsid protein (Cp) dimer, previously determined by cryo-electron microscopy (Conway et al. (1997), Böttcher et al. (1997)). In both proteins, dimerization is effected by formation of a four-helix bundle, whereby each subunit contributes a helix-loop-helix and most of the interaction between subunits is mediated by one pair of helices. These are the first two observations of a motif that is common to the capsid proteins of two enveloped viruses and quite distinct from the eight-stranded anti-parallel beta-barrel found in most other virus capsid proteins solved to date (Harrison et al. (1996)). Motivated by the structural resemblance, we have examined retroviral and HBV capsid protein sequences and found weak but significant similarities between them. These similarities further support an evolutionary relationship between these two virus families of great medical importance -- the hepadnaviruses (e.g. HBV) and retroviruses (e.g. HIV).

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Zlotnick A,Stahl SJ,Wingfield PT,Conway JF,Cheng N,Steven AC

doi

10.1016/s0014-5793(98)00755-8

subject

Has Abstract

pub_date

1998-07-24 00:00:00

pages

301-4

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00755-8

journal_volume

431

pub_type

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