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A viral ER-resident glycoprotein inactivates the MHC-encoded peptide transporter.

Abstract：

:Human cytomegalovirus inhibits peptide import into the endoplasmic reticulum (ER) by the MHC-encoded TAP peptide transporter. We identified the open reading frame US6 to mediate this effect. Expression of the 21 kDa US6 glycoprotein in human cytomegalovirus-infected cells correlates with the inhibition of peptide transport during infection. The subcellular localization of US6 is ER restricted and is identical with TAP. US6 protein is found in complexes with TAP1/2, MHC class I heavy chain, beta2-microglobulin, calnexin, calreticulin, and tapasin. TAP inhibition, however, is independent of the presence of class I heavy chain and tapasin. The results establish a new mechanism for viral immune escape and a novel role for ER-resident proteins to regulate TAP via its luminal face.

journal_name

Immunity

journal_title

Immunity

authors

Hengel H,Koopmann JO,Flohr T,Muranyi W,Goulmy E,Hämmerling GJ,Koszinowski UH,Momburg F

doi

10.1016/s1074-7613(00)80350-7

subject

Has Abstract

pub_date

1997-05-01 00:00:00

pages

623-32

issue

5

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(00)80350-7

journal_volume

6

pub_type

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