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   <subfield code="a">N -Glycosylation contributes to the limited cross-reactivity between hemagglutinin neuraminidase proteins of human parainfluenza virus type 4A and 4B</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Hiroshi Komada, Morihiro Ito, Machiko Nishio, Mitsuo Kawano, Hisataka Ohta, Masato Tsurudome, Shigeru Kusagawa, Myles O'Brien, Hisanori Bando, Yasuhiko Ito]</subfield>
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   <subfield code="a">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.</subfield>
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   <subfield code="a">Springer-Verlag Berlin Heidelberg, 2000</subfield>
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   <subfield code="a">Key words Human parainfluenza virus type 4 hemagglutinin neuraminidase protein</subfield>
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   <subfield code="a">N-Glycosylation site</subfield>
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   <subfield code="D">Hiroshi</subfield>
   <subfield code="u">Department of Microbiology, Mie University School of Medicine, Tsu, Mie 514-8507, Japan e-mail: ito@doc.medic.mie-u.ac.jp; Fax: +81-59-2315008, JP</subfield>
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   <subfield code="u">Department of Microbiology, Mie University School of Medicine, Tsu, Mie 514-8507, Japan e-mail: ito@doc.medic.mie-u.ac.jp; Fax: +81-59-2315008, JP</subfield>
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   <subfield code="u">Department of Microbiology, Mie University School of Medicine, Tsu, Mie 514-8507, Japan e-mail: ito@doc.medic.mie-u.ac.jp; Fax: +81-59-2315008, JP</subfield>
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   <subfield code="u">Department of Microbiology, Mie University School of Medicine, Tsu, Mie 514-8507, Japan e-mail: ito@doc.medic.mie-u.ac.jp; Fax: +81-59-2315008, JP</subfield>
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   <subfield code="u">Department of Microbiology, Mie University School of Medicine, Tsu, Mie 514-8507, Japan e-mail: ito@doc.medic.mie-u.ac.jp; Fax: +81-59-2315008, JP</subfield>
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   <subfield code="u">Department of Microbiology, Mie University School of Medicine, Tsu, Mie 514-8507, Japan e-mail: ito@doc.medic.mie-u.ac.jp; Fax: +81-59-2315008, JP</subfield>
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   <subfield code="u">Department of Microbiology, Mie University School of Medicine, Tsu, Mie 514-8507, Japan e-mail: ito@doc.medic.mie-u.ac.jp; Fax: +81-59-2315008, JP</subfield>
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