Type II integral membrane protein, TM of J paramyxovirus promotes cell-to-cell fusion

Zhuo Li, Cher Hung, Reay G. Paterson, Frank Michel, Sandra Fuentes, Ryan Place, Yuan Lin, Robert J. Hogan, Robert A. Lamb, Biao He*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Paramyxoviruses include many important animal and human pathogens. Most paramyxoviruses have two integral membrane proteins: fusion protein (F) and attachment proteins hemagglutinin, hemagglutinin-neuraminidase, or glycoprotein (G), which are critical for viral entry into cells. J paramyxovirus (JPV) encodes four integral membrane proteins: F, G, SH, and transmembrane (TM). The function of TM is not known. In this work, we have generated a viable JPV lacking TM (JPV?TM). JPV?TM formed opaque plaques compared with JPV. Quantitative syncytia assays showed that JPV?TM was defective in promoting cell-to-cell fusion (i.e., syncytia formation) compared with JPV. Furthermore, cells separately expressing F, G, TM, or F plus G did not form syncytia whereas cells expressing F plus TM formed some syncytia. However, syncytia formation was much greater with coexpression of F, G, and TM. Biochemical analysis indicates that F, G, and TM interact with each other. A small hydrophobic region in the TM ectodomain from amino acid residues 118 to 132, the hydrophobic loop (HL), was important for syncytial promotion, suggesting that the TM HL region plays a critical role in cell-to-cell fusion.

Original languageEnglish (US)
Pages (from-to)12504-12509
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number40
StatePublished - Oct 6 2015


  • Fusion
  • J paramyxovirus
  • Syncytia
  • TM

ASJC Scopus subject areas

  • General


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