Sequence and structural analyses of NSP4 proteins from human group A rotavirus strains detected in Tunisia

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• 作者：M. Ben Hadj Fredj^a ; ^b ; M. Ben Hamida-Rebaï ; ^a ; ^b ; M. Zeller^c ; E. Heylen^c ; M. Van Ranst^c ; J. Matthijnssens^c ; A. Trabelsi^a ; ^b ; ^{abdelhalim.trabelsi@gmail.com" class="auth_mail}
• 关键词：Rotavirus ; NSP4 ; Domain ; Genotype ; Aminoacid variations
• 刊名：Pathologie Biologie
• 出版年：June 2014
• 年：2014
• 卷：62
• 期：3
• 页码：146-151
• 全文大小：2023 K

文摘

The NSP4 protein of group A rotavirus (RVA) has been recognized as a viral enterotoxin and plays important roles in viral pathogenesis and morphogenesis. Domains involved in structural and functional interactions have been proposed mainly based on the simian SA11 strain.

Methods

NSP4 has been classified into 15 different genotypes (E1-E15), and the aim of this study was to analyze the sequences of 46 RVA strains in order to determine the aminoacid (aa) differences between E1 and E2 genotypes. Another aspect was to characterize the structural and physicochemical properties of these strains.

Results

Comparison of deduced aa sequences of the NSP4 protein showed that divergences between NSP4 genotypes E1 and E2 were mostly observed in the VP4-binding, the interspecies variable domain (ISVD) and the double-layered particle (DLP) binding domains. Interestingly, uncommon variations in residues 131 and 138, which are known to be important aa in pathogenesis, were found in one unusual animal derived strain belonging to the E2 genotype. Concerning the structural aspect, no significant differences were noted.

Conclusion

The presence of punctual aa variations in the NSP4 genotypes may indicate that NSP4 mutates mainly via accumulation of point mutations.