tetano
Editor, Senior Moderator
Jpn J Infect Dis. 2013;66(6):526-9.
Protease-Dependent Hemagglutinin Cleavage Contributes to Alteration in Chicken Hemagglutination by the H3N2 Influenza A Virus.
Yamaoka M, Makino A, Sasahara K, Nastri AM, Krisna LA, Purhito EF, Poetranto ED, Wulandari L, Yudhawati R, Setiawati L, Setyoningrum RA, Shinya K.
Source
Center for Infectious Diseases, Graduate School of Medicine, Kobe University.
Abstract
The human influenza A virus (H3N2) has been the predominant influenza strain since 1992, and one property of this virus is non-agglutination of chicken erythrocytes [Ch(-) virus]. The Ch(-) virus in our study was able to acquire chicken hemagglutination [Ch(+)] by trypsin passage but not by chymotrypsin passage. Moreover, the trypsin-passaged Ch(+) viruses reacquired the Ch(-) property after a further chymotrypsin passage. In particular, genetic analysis showed no evidence of mutations in the hemagglutinin (HA) gene during either trypsin or chymotrypsin passages: the only differences found were in the HA cleavage sites between the trypsin-passaged virus and the chymotrypsin-passaged virus as determined by the N-terminal amino acid sequence. These results suggested that protease-dependent differences at the viral HA cleavage site, rather than genetic mutations, are likely to have a significant effect on the viral ability to produce chicken hemagglutination.
PMID:
24270143
[PubMed - in process]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed?term=Purhito EF[Author]&cauthor=true&cauthor_uid=24270143
Protease-Dependent Hemagglutinin Cleavage Contributes to Alteration in Chicken Hemagglutination by the H3N2 Influenza A Virus.
Yamaoka M, Makino A, Sasahara K, Nastri AM, Krisna LA, Purhito EF, Poetranto ED, Wulandari L, Yudhawati R, Setiawati L, Setyoningrum RA, Shinya K.
Source
Center for Infectious Diseases, Graduate School of Medicine, Kobe University.
Abstract
The human influenza A virus (H3N2) has been the predominant influenza strain since 1992, and one property of this virus is non-agglutination of chicken erythrocytes [Ch(-) virus]. The Ch(-) virus in our study was able to acquire chicken hemagglutination [Ch(+)] by trypsin passage but not by chymotrypsin passage. Moreover, the trypsin-passaged Ch(+) viruses reacquired the Ch(-) property after a further chymotrypsin passage. In particular, genetic analysis showed no evidence of mutations in the hemagglutinin (HA) gene during either trypsin or chymotrypsin passages: the only differences found were in the HA cleavage sites between the trypsin-passaged virus and the chymotrypsin-passaged virus as determined by the N-terminal amino acid sequence. These results suggested that protease-dependent differences at the viral HA cleavage site, rather than genetic mutations, are likely to have a significant effect on the viral ability to produce chicken hemagglutination.
PMID:
24270143
[PubMed - in process]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed?term=Purhito EF[Author]&cauthor=true&cauthor_uid=24270143