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Journal of Virology, September 2008, p. 8283-8295, Vol. 82, No. 17
0022-538X/08/$08.00+0     doi:10.1128/JVI.00460-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Effects of Hemagglutinin-Neuraminidase Protein Mutations on Cell-Cell Fusion Mediated by Human Parainfluenza Type 2 Virus{triangledown}

Masato Tsurudome,1* Machiko Nishio,1 Morihiro Ito,2 Shunsuke Tanahashi,1 Mitsuo Kawano,1 Hiroshi Komada,3 and Yasuhiko Ito2

Department of Microbiology, Mie University Graduate School of Medicine, 2-174 Edobashi, Tsu, Mie 514-8507, Japan,1 Department of Biomedical Sciences, College of Life and Health Sciences, Chubu University, 1200 Matsumoto-Cho, Kasugai, Aichi 487-8501, Japan,2 Department of Microbiology, Suzuka University of Medical Science and Technology, 1001-1 Kishioka-Cho, Suzuka, Mie 510-0226, Japan3

Received 3 March 2008/ Accepted 6 June 2008

The monoclonal antibody M1-1A, specific for the hemagglutinin-neuraminidase (HN) protein of human parainfluenza type 2 virus (HPIV2), blocks virus-induced cell-cell fusion without affecting the hemagglutinating and neuraminidase activities. F13 is a neutralization escape variant selected with M1-1A and contains amino acid mutations N83Y and M186I in the HN protein, with no mutation in the fusion protein. Intriguingly, F13 exhibits reduced ability to induce cell-cell fusion despite its multistep replication. To investigate the potential role of HPIV2 HN protein in the regulation of cell-cell fusion, we introduced these mutations individually or in combination to the HN protein in the context of recombinant HPIV2. Following infection at a low multiplicity, Vero cells infected with the mutant virus H-83/186, which carried both the N83Y and M186I mutations, remained as nonfused single cells at least for 24 h, whereas most of the cells infected with wild-type virus mediated prominent cell-cell fusion within 24 h. On the other hand, the cells infected with the mutant virus, carrying either the H-83 or H-186 mutation, mediated cell-cell fusion but less efficiently than those infected with wild-type virus. Irrespective of the ability to cause cell-cell fusion, however, every virus could infect all the cells in the culture within 48 h after the initial infection. These results indicated that both the N83Y and M186I mutations in the HN protein are involved in the regulation of cell-cell fusion. Notably, the limited cell-cell fusion by H-83/186 virus was greatly promoted by lysophosphatidic acid, a stimulator of the Ras and Rho family GTPases.

* Corresponding author. Mailing address: Department of Microbiology, Mie University Graduate School of Medicine, 2-174 Edobashi, Tsu, Mie 514-8507 Japan. Phone and fax: 81 59 231 5413. E-mail: turudome{at}doc.medic.mie-u.ac.jp

{triangledown} Published ahead of print on 18 June 2008.

Journal of Virology, September 2008, p. 8283-8295, Vol. 82, No. 17
0022-538X/08/$08.00+0     doi:10.1128/JVI.00460-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Okada, H., Itoh, M., Nagata, K., Takeuchi, K. (2009). Previously Unrecognized Amino Acid Substitutions in the Hemagglutinin and Fusion Proteins of Measles Virus Modulate Cell-Cell Fusion, Hemadsorption, Virus Growth, and Penetration Rate. J. Virol. 83: 8713-8721 [Abstract] [Full Text]  


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