N-Glycosylation contributes to the limited cross-reactivity between hemagglutinin neuraminidase proteins of human parainfluenza virus type 4A and 4B

Hiroshi Komada, Morihiro Ito, Machiko Nishio, Mitsuo Kawano, Hisataka Ohta, Masato Tsurudome, Shigeru Kusagawa, Myles O'Brien, Hisanori Bando, Yasuhiko Ito

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

cDNAs encoding human parainfluenza virus type 4B (hPIV-4B) hemagglutinin neuraminidase (HN) protein were cloned and the nucleotide sequences were determined. A high degree of identity (81.4%) was observed between the nucleotide sequences of hPIV-4A and -4B HN proteins, and an 87.3% identity was found between the deduced amino acid sequences. This degree of identity is considered to be greater than immunological similarity between hPIV-4A and -4B HN proteins determined using monoclonal antibodies. To elucidate the causes of the antigenic difference between HN proteins of hPIV-4A and -4B, we constructed three cDNAs of hPIV-4B HN whose potential N-glycosylation sites were partially or completely the same as in hPIV-4A HN cDNA. We compared the antigenicity of the expressed wild-type and mutant proteins, and found that the antigenicities of the mutant hPIV-4B HN proteins were more similar to the hPIV-4A HN protein than to the non-mutant hPIV-4B HN protein. This study indicated that the antigenic diversity between hPIV-4A and -4B was partly caused by deletion or creation of glycosylation sites, showing that the point mutations resulting in deletion or creation of glycosylation sites is one of the initial steps leading to the division of virus into subtypes.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalMedical Microbiology and Immunology
Volume189
Issue number1
DOIs
Publication statusPublished - 1 Jan 2000

Keywords

  • Antigenicity
  • Human parainfluenza virus type 4 hemagglutinin neuraminidase protein
  • N-Glycosylation site

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