Genetic characteristics analysis of the hemagglutinin gene of measles virus in Shanghai， 2001‒2018
10.19428/j.cnki.sjpm.2022.21459
- VernacularTitle:2001—2018年上海市麻疹病毒流行株血凝素基因特征分析
- Author:
Yuying YANG
1
;
Dayu CHEN
2
;
Wei TANG
1
;
Yunyi LI
1
;
Jiayu WANG
1
;
Shupei LI
1
;
Chongshan LI
3
Author Information
1. Shanghai Municipal Center for Disease Control and Prevention, Shanghai 200336, China
2. Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China
3. Shanghai Institute of Infectious Disease and Biosecurity, Shanghai 200032, China
- Publication Type:Journal Article
- Keywords:
measles virus;
hemagglutinin;
phylogenetic analysis;
amino acid variation
- From:
Shanghai Journal of Preventive Medicine
2022;34(5):436-440
- CountryChina
- Language:Chinese
-
Abstract:
ObjectiveTo analyze the genetic characteristics of the hemagglutinin （H） gene of measles virus （MeV） in Shanghai， 2001‒2018. MethodsNasopharyngeal swab specimens were collected from suspected measles cases reported in Shanghai from 2001 to 2018， and the isolation of measles virus was conducted with Vero/hSLAM cell line. RT-PCR amplification and sequencing were conducted after RNA extraction to analyze the genetic characteristics of the complete H gene. ResultsIn total， 5 665 nasopharyngeal swab samples were collected by suspected measles case surveillance from 2001 to 2018， and 1 394 measles virus strains were isolated. The homology of nucleotide acid and amino acid among 349 representative measles virus isolates was 87.4%‒100.0% and 85.1%‒100.0%， respectively. The homology of nucleotide acid and amino acid between representative measles virus isolates and China vaccine strain （S191） was 85.7%‒100.0% and 84.1%‒100.0%， respectively. All the sub-genotype H1a MeV isolates had an amino acid substitution （Ser240Asn）， which removed a predicted N-linked glycosylation site. ConclusionMost of the MeV isolates are sub-genotype H1a analyzed based on H gene， which are identical to those of the N gene. The predicted amino acid sequences of the H protein are relatively conserved at most of the functionally significant amino acid positions.
