Title

Structure function studies on different structural domains of nucleoprotein of H1N1 subtype

Authors

Parveen Salahuddin¹, Asad U. Khan^{1, 2*}

Affiliation

¹Distributed Information Sub-Centre; ²Interdisciplinary Biotechnology Unit; A.M.U. Aligarh, 202002, India

Email

asad.k@rediffmail.com

+91 571 2723088

+91 571 2721776; * Corresponding author

Article Type

Hypothesis

Date

received April 04, 2010; accepted June 08, 2010, published June 24, 2010
 

Recent 2009 flu pandemic is a global outbreak of a new strain of influenza A virus subtype H1N1. The H1N1 virus has crossed species barrier to human and apparently acquired the capability to transmit this disease from human to human. The NP is a multifunctional protein that not only encapsidates viral RNA (vRNA), but also forms homo-oligomer and thereby maintains RNP structure. It is also thought to be the key adaptor for virus and host cell interaction. Thus, it is one of the factor that play a key role in the pathogenesis of influenza A virus infection. Therefore, to understand the cause of pathogenicity of H1N1 virus, we have studied the structure-function relationship of different domains of NP. Our results showed that conservative mutation in NP of various strains were pathogenic in nature. However, non-conservative mutation slightly abrogated oligomerization and was therefore less pathogenic. Our results also suggest that beside tail and body domain, head domain may also participate in an oligomerization process.

Keywords

antigenic site; nucleoprotein; swine flu; H1N1; pathogenicity

Citation

Salahuddin & Khan, Bioinformation, 5 (1) 25-30, 2010

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.