Antigenicity and Hemaglutination Activity of a Recombinant Hemagglutinin-Neuraminidase of Paramyxovirus Tianjin Strain

Paramyxovirus Tianjin strain, a new genotype of Sendai virus, was isolated from the lungs of common cotton-eared marmoset that died of severe respiratory infection in the marmoset colonies. The 19.28% IgM positive rate in the young children with acute respiratory tract infection suggested a close re...

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Published inVirologica Sinica Vol. 23; no. 4; pp. 287 - 294
Main Authors Li, Mei, Yuan, Li-jun, Shi, Li-ying, Li, Xiao-mian, Wang, Qing, Wang, Wen-xiu
Format Journal Article
LanguageEnglish
Chinese
Published Heidelberg SP Wuhan Institute of Virology, CAS 01.08.2008
Department of Microbiology, Tianjin Medical University, Tianjin 300070, China
Subjects
Biochemistry
Biomedical and Life Sciences
Biomedicine
Callithrix
Influenza virus
Medical Microbiology
Microbial Genetics and Genomics
Microbiology
Oncology
Paramyxovirus
Sendai virus
Virology
仙台病毒
副粘病毒天津变种
抗原性
神经氨酸酶
红血球凝聚素
Hemagglutinin-neuraminidase
Hemagglutination
Antigenicity
Sendai virus
Paramyxovirus Tianjin strain
S852.65
Sendal virus
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Summary:Paramyxovirus Tianjin strain, a new genotype of Sendai virus, was isolated from the lungs of common cotton-eared marmoset that died of severe respiratory infection in the marmoset colonies. The 19.28% IgM positive rate in the young children with acute respiratory tract infection suggested a close relationship between Tianjin strain and humans. Hemagglutinin-neuraminidase （HN） is its major transmembrane glycoprotein responsible for viral attachment, penetration and release. To clear the relationship between HN structure and function of paramyxovirus Tianjin strain, rHN1, rHN2 and rHN3 overlapping the ectodomain of HN protein were expressed. Their antigenicity and hemaglutination activity, as well as cross reactivity to standard antisera against influenza virus type A, type B were analyzed. The results indicated expressed rHNs have the natural antigenicity The segment rHN2 possesses more linear epitopes exposed on the surface of the native HN protein than found in segments rHN3 and rHN1. The hemagglutination activity of segment rHN3 is higher than that of segments rHN2 and rHN1, and partially dependent on the three-dimensional conformation of HN3 protein. Cross-reactivity between rHNs and standard antisera against influenza virus type A, type B suggested that rHNs might not be the best alternative as specific antigens to detect virus in clinical serum specimens,
Bibliography:Hemagglutinin-neuraminidase
Hemagglutination
Antigenicity
Sendai virus
42-1760/Q
Paramyxovirus Tianjin strain; Sendai virus; Hemagglutinin-neuraminidase; Hemagglutination;Antigenicity
Paramyxovirus Tianjin strain
S852.65
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1674-0769
1995-820X
DOI:10.1007/s12250-008-2965-4