Abstract：
:The hemagglutinin (HA) of avian influenza viruses plays a very important role in the infection of host cells. In this study, the HA gene of the highly pathogenic avian influenza H5N1 virus was cloned and expressed in silkworm larvae. The expressed recombinant HA (rHA) was purified using fetuin-agarose chromatography and Superdex 200 10/300 GL gel filtration chromatography, and the identity of purified rHA was confirmed by SDS-PAGE and Western blot. Approximately 500 μg of purified rHA was obtained from a total of 30 silkworm larvae, suggesting the high efficiency of the silkworm expression system. The purified rHA bound to a rabbit polyclonal antibody against influenza A virus H5N1 (avian flu) HA, suggesting its antigenicity and potential application in vaccine development. Gel filtration chromatography showed that purified HA was present in the void volume fractions, indicating that rHA may form an oligomer. The rHA bound to poly{Neu5Acα2,3LacNAcβ-O[(CH₂)₅NHCO]₂(CH₂)₅NH-/γ-PGA}, which mimics an avian type receptor, but did not bind to γ-polyglutamic acid or human type receptor mimic, poly{Neu5Acα2,6LacNAcβ-O[(CH₂)₅NHCO]₂(CH₂)₅NH-/γ-PGA}, suggesting that it could be utilized as a blocking agent against infection by highly pathogenic influenza viruses.
journal_name
J Virol Methodsjournal_title
Journal of virological methodsauthors
Dong J,Harada M,Yoshida S,Kato Y,Murakawa A,Ogata M,Kato T,Usui T,Park EYdoi
10.1016/j.jviromet.2013.08.040subject
Has Abstractpub_date
2013-12-01 00:00:00pages
271-6issue
1-2eissn
0166-0934issn
1879-0984pii
S0166-0934(13)00387-Xjournal_volume
194pub_type
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