tetano
Editor, Senior Moderator
Virus Genes. 2013 Oct 31. [Epub ahead of print]
Loss and gain of N-linked glycosylation sites in globular head and stem of HA found in A/H3N2 flu fatal and severe cases during 2013 Tunisia flu seasonal survey.
El Moussi A, Ben Hadj Kacem MA, Slim A.
Source
National Influenza Centre-Tunis, Microbiology Laboratory, Charles Nicolle's Hospital, Bvd 9 avril, Tunis, Tunisia, awatefbio@ymail.com.
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.
PMID:
24174280
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24174280
Loss and gain of N-linked glycosylation sites in globular head and stem of HA found in A/H3N2 flu fatal and severe cases during 2013 Tunisia flu seasonal survey.
El Moussi A, Ben Hadj Kacem MA, Slim A.
Source
National Influenza Centre-Tunis, Microbiology Laboratory, Charles Nicolle's Hospital, Bvd 9 avril, Tunis, Tunisia, awatefbio@ymail.com.
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.
PMID:
24174280
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24174280