Mutational changes in the hemagglutinin of equine H3 influenza viruses result in the introduction of a glycosylation site which enhances the infectivity of the viruses.
Abstract: The complete amino acid sequences of the hemagglutinin (HA) glycoprotein of three equine-2 influenza viruses from tropical Africa are presented in comparison with that of a well characterized European equine-2 virus (Suffolk/89) and a consensus sequence from the database. The sequences of the tropical African viruses were deduced from the complete nucleotide sequences of their HA genes reported earlier. Mutational changes in the nucleotide sequences resulted in amino acid changes in the HA which led to the introduction of a new asparagine-linked (N-linked) glycosylation site in two viruses. This new glycosylation site enhanced the infectivity of these viruses as investigated by plaque assay, virus titration in embryonated chicken eggs and tunicamycin treatment. The role of N-linked glycosylation of influenza virus HA glycoprotein in virus infectivity, antigenicity and immunogenicity is discussed in the light of the results of our previous and present investigations.
Publication Date: 1997-01-01 PubMed ID: 9449785DOI: 10.1007/BF02816955Google Scholar: Lookup
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- Comparative Study
- Journal Article
Summary
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The research article examines the impact of mutational changes in the hemagglutinin of equine H3 influenza viruses, indicating these alterations can introduce a new glycosylation site and consequently heighten the infectivity of the viruses.
Objective and Methodology of the Research
- The researchers’ primary objective was to investigate the effect of mutational changes in the hemaglutinin (HA) gene on the infectivity of equine H3 influenza viruses.
- The study made use of three equine-2 influenza viruses from tropical Africa. The HA glycoprotein sequences of these viruses were compared with a well-known European equine-2 virus (Suffolk/89) and a consensus sequence from the database.
- Researchers obtained the sequences of the tropical African viruses from the complete nucleotide sequences of their HA genes reported in past studies.
Results of the Research
- Based on their investigation, the researchers found that mutational changes at the nucleotide level resulted in alterations at the amino acid level in the HA.
- These amino acid changes led to the introduction of new asparagine-linked (N-linked) glycosylation sites in two of the viruses.
- The emergent glycosylation site boosted the infectivity of these viruses. The researchers confirmed this increase in infectivity through plaque assay, virus titration in embryonated chicken eggs, and tunicamycin treatment.
Implications and Conclusions
- The research further emphasizes the role of N-linked glycosylation in the influenza virus HA glycoprotein, especially regarding virus infectivity, antigenicity, and immunogenicity.
- The study results were discussed in view of previous and current investigations, highlighting the evolving understanding of the molecular biology of influenza viruses.
- The findings could potentially guide future research and interventions aimed at controlling and combating the spread of equine H3 influenza viruses.
Cite This Article
APA
Adeyefa CA, McCauley JW, Tomori O.
(1997).
Mutational changes in the hemagglutinin of equine H3 influenza viruses result in the introduction of a glycosylation site which enhances the infectivity of the viruses.
Folia Microbiol (Praha), 42(4), 390-394.
https://doi.org/10.1007/BF02816955 Publication
Researcher Affiliations
- Institute for Animal Health, Pirbright Laboratory, Surrey, United Kingdom.
MeSH Terms
- Amino Acid Sequence
- Animals
- Asparagine / chemistry
- Cells, Cultured
- Chick Embryo
- Consensus Sequence
- Cytopathogenic Effect, Viral
- Glycosylation / drug effects
- Hemagglutinin Glycoproteins, Influenza Virus / chemistry
- Hemagglutinin Glycoproteins, Influenza Virus / genetics
- Hemagglutinin Glycoproteins, Influenza Virus / physiology
- Influenza A virus / genetics
- Influenza A virus / pathogenicity
- Molecular Sequence Data
- Nigeria
- Protein Processing, Post-Translational / drug effects
- Sequence Alignment
- Sequence Homology, Amino Acid
- Tunicamycin / pharmacology
- Virulence / genetics
References
This article includes 12 references
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