Abstract:
:Glycosylation on the globular head of the hemagglutinin (HA) protein of influenza virus acts as an important target for recognition and destruction of virus by innate immune proteins of the collectin family. In the current study, we have characterized the dynamic amino acid changes at N-linked glycosylation sites of full length sequences of HA genes of 5 A/H3N2 Tunisian strains isolates from mild, severe, and fatal cases. Compared to the reference strain, A/Perth/16/2009 substitutions in potential N-glycosylation sites were observed in 5 HA genes at five different positions (45, 124, 128, 144, and 145) generating the losses and gains of N-linked glycosylation sites. Also the mutation N145S was presented in the receptor-binding site of all segments analyzed. Point mutations in several positions in the gene encoding the H3 of Tunisian strains were shown to ablate a glycan attachment site and also loss of a potential glycosylation site. The relation between these mutations and virulence of influenza A/H3N2 virus needed to be verified in the further experiments.
journal_name
Virus Genesjournal_title
Virus genesauthors
El Moussi A,Ben Hadj Kacem MA,Slim Adoi
10.1007/s11262-013-0993-0subject
Has Abstractpub_date
2014-02-01 00:00:00pages
189-92issue
1eissn
0920-8569issn
1572-994Xjournal_volume
48pub_type
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