Influenza A(H1N1)pdm09 Virus

Therapeutics and Challenges

Shailendra K Saxena; Rosaiah Kotikalapudi; Sneham Tiwari; Charuvaka Muvva


Future Virology. 2012;7(10):947-950. 

In This Article

Molecular Mechanisms & Ramifications

Different influenza viruses possess differing antigenic properties, specifically for binding to the sialyl moiety of host cells. With the aid of envelope glycoprotein HA, influenza viruses can easily bind to cell-surface glycosylated oligosaccharides that have sialic acids at their terminals, although this binding is very specific. This specificity acts as a host barrier against viral transmission. Some strains have the capacity to bind to both glycan linkages, making them more virulent and resulting in various intestinal illnesses. Mutations in the HA region of a virus may alter its binding affinity to the host through antigenic shift, leading to differential pathogenesis among different strains.[6] Several studies have examined the underlying molecular mechanisms of viral attack. HA helps the virus to attach to the sialic acid receptor of the host cell, which is followed by endocytosis. Viral RNA polymerase transcribes the viral genome and releases the mRNA for further processing. Viral genomic ssRNA synthesis takes place after mRNA release by exploiting host cellular machinery. This is then followed by assembly, maturation and ultimately by the production of progeny virions via budding from the infected host cell membrane.[1]