Transport of cationic amino acids by the mouse ecotropic retrovirus receptor.

Abstract:

:Susceptibility of rodent cells to infection by ecotropic murine leukaemia viruses (MuLV) is determined by binding of the virus envelope to a membrane receptor that has multiple membrane-spanning domains. Cells infected by ecotropic MuLV synthesize envelope protein, gp70, which binds to this receptor, thereby preventing additional infections. The consequences of envelope-MuLV receptor binding for the infected host cell have not been directly determined, partly because the cellular function of the MuLV receptor protein is unknown. Here we report a coincidence in the positions of the first eight putative membrane-spanning domains found in the virus receptor and in two related proteins, the arginine and histidine permeases of Saccharomyces cerevisiae (Fig. 1), but not in any other proteins identified by computer-based sequence comparison of the GenBank data base. Xenopus oocytes injected with receptor-encoding messenger RNA show increased uptake of L-arginine, L-lysine and L-ornithine. The transport properties and the expression pattern of the virus receptor behave in ways previously attributed to y+, the principal transporter of cationic L-amino acids in mammalian cells.

journal_name

Nature

journal_title

Nature

authors

Kim JW,Closs EI,Albritton LM,Cunningham JM

doi

10.1038/352725a0

keywords:

subject

Has Abstract

pub_date

1991-08-22 00:00:00

pages

725-8

issue

6337

eissn

0028-0836

issn

1476-4687

journal_volume

352

pub_type

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