Deletion of gpUL132, a structural component of human cytomegalovirus, results in impaired virus replication in fibroblasts.

Abstract:

:The coding capacity of human cytomegalovirus (HCMV) for glycoproteins by far exceeds that of other herpesviruses. Few of these proteins have been characterized so far. We have investigated the gene product of reading frame UL132. The putative protein product of UL132 is a glycoprotein with a theoretical mass of 29.8 kDa. Transcription analysis revealed that the gene is transcribed with a true late kinetics from the laboratory-adapted strain AD169 and the low-passage isolate TB40E. Two proteins of 22 to 28 kDa and 45 to 60 kDa were detected in virus-infected cells as well as in extracellular virions. The larger protein carried N-linked carbohydrates. Both protein forms were present in laboratory-adapted strains as well as in low-passage isolates of HCMV. Recombinant viruses with the UL132 gene deleted were constructed in the low-passage HCMV isolate PAN as well as the high-passage isolate AD169. Deletion of UL132 from either genome resulted in a pronounced replication deficit with a reduction of approximately 100-fold for HCMV strain AD169. Thus, the protein product of the UL132 reading frame represents a structural viral glycoprotein of HCMV that has an important function for viral replication in tissue culture.

journal_name

J Virol

journal_title

Journal of virology

authors

Spaderna S,Kropff B,Ködel Y,Shen S,Coley S,Lu S,Britt W,Mach M

doi

10.1128/JVI.79.18.11837-11847.2005

subject

Has Abstract

pub_date

2005-09-01 00:00:00

pages

11837-47

issue

18

eissn

0022-538X

issn

1098-5514

pii

79/18/11837

journal_volume

79

pub_type

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