An endoplasmic reticulum protein, p180, is highly expressed in human cytomegalovirus-permissive cells and interacts with the tegument protein encoded by UL48

K. Ogawa-Goto, S. Irie, A. Omori, Y. Miura, H. Katano, H. Hasegawa, T. Kurata, T. Sata, Yujiro Arao

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

We have used a virus overlay assay to detect cellular proteins associated with human cytomegalovirus (HCMV) particles. The radiolabeled HCMV particles specifically bound to two host proteins with molecular sizes of 150 and 180 kDa. By a micro-amino-acid sequencing technique, the 180-kDa protein was identified as a human homologue of the ES130/p180 ribosome receptor (p180), which is an integral endoplasmic reticulum (ER) membrane protein possessing a very unique tandem repeat domain at its N-terminal region. The virus overlay assay using truncated p180 polypeptides revealed that HCMV binding to human p180 occurred through the N-terminal region. In HCMV-permissive cells the high level of expression of the human p180 protein was clearly observed regardless of cell type. Furthermore, we showed that p180 binds to the UL48 gene product, which is one of the predominant tegument proteins of HCMV and which is considered to be tightly associated with the capsid. The interaction between the two proteins was assumed to be specific and was observed both in vitro and in vivo. During the late phase of infection, the unique relocation of human p180 was observed, that is, to the juxtanuclear region, which appeared to be in the vicinity of the area where naked virions were frequently observed in an electron-microscopic study. Thus our data suggest that p180 interacts with the HCMV tegument, at least through pUL48, during the HCMV replication process. We discuss the possible role of the interaction between p180 and pUL48 in the intracellular transport of HCMV virions.

Original languageEnglish
Pages (from-to)2350-2362
Number of pages13
JournalJournal of Virology
Volume76
Issue number5
DOIs
Publication statusPublished - 2002
Externally publishedYes

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Human herpesvirus 5
Cytomegalovirus
Endoplasmic Reticulum
endoplasmic reticulum
Proteins
proteins
cells
virion
Virion
viruses
capsid
tandem repeat sequences
assays
ribosomes
membrane proteins
Viruses
polypeptides
Tandem Repeat Sequences
Capsid
Protein Sequence Analysis

ASJC Scopus subject areas

  • Immunology

Cite this

An endoplasmic reticulum protein, p180, is highly expressed in human cytomegalovirus-permissive cells and interacts with the tegument protein encoded by UL48. / Ogawa-Goto, K.; Irie, S.; Omori, A.; Miura, Y.; Katano, H.; Hasegawa, H.; Kurata, T.; Sata, T.; Arao, Yujiro.

In: Journal of Virology, Vol. 76, No. 5, 2002, p. 2350-2362.

Research output: Contribution to journalArticle

Ogawa-Goto, K. ; Irie, S. ; Omori, A. ; Miura, Y. ; Katano, H. ; Hasegawa, H. ; Kurata, T. ; Sata, T. ; Arao, Yujiro. / An endoplasmic reticulum protein, p180, is highly expressed in human cytomegalovirus-permissive cells and interacts with the tegument protein encoded by UL48. In: Journal of Virology. 2002 ; Vol. 76, No. 5. pp. 2350-2362.
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AU - Irie, S.

AU - Omori, A.

AU - Miura, Y.

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