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Current Analytical Chemistry

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ISSN (Print): 1573-4110
ISSN (Online): 1875-6727

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Research Article

A Bioinformatics Study of the Influenza H5N1 Virus that Infects Wild Fowl and Poultry and, Potentially, Humans

Author(s): Carlos Polanco*, Vladimir N. Uversky, Alberto Huberman, Enrique Hernandez-Lemus, Mireya Martínez-Garcia, Claudia Pimentel Hernández, Martha Rios Castro, Thomas Buhse, Gilberto Vargas Alarcon, Jorge Alberto Castañón González, Juan Luciano Díaz González, Mauricio Missael Sanchez Díaz, Erika Jeannette López Oliva, Francisco J. Roldan Gomez and Brayans Becerra Luna

Volume 19, Issue 10, 2023

Published on: 08 December, 2023

Page: [743 - 764] Pages: 22

DOI: 10.2174/0115734110271243231123160146

Price: $65

Abstract

Introduction: More than sixteen countries are infected with the highly pathogenic avian influenza A-H5N1 virus. As the virus circles the world, it has led to the slaughter of millions of poultry birds as well as the infection of farmed mink in Europe and among seals and grizzly bears on the Northern coast of America; some infected mammals exhibited neurological symptoms like disorientation and blindness, which marks the first large H5N1 outbreak potentially driven by mammal-tomammal transmission that could be poised to spillover into humans its mortality rate in humans exceeds 50%. The virus pandemic potential is continuously monitored to characterize further and analyze its zoonotic potential (PAHO/WHO, March 2023).

Objective: To gain comprehension of the envelope glycoproteins that express H5N1 influenza (hemagglutinin and neuraminidase proteins), computational studies were carried out.

Methods: Calculating each sequence's Protein Intrinsic Disorder Predisposition (PIDP) and Polarity Index Method Profile 2.0 v (PIM 2.0 v) required the employment of multiple computer algorithms.

Results: The analysis of the PIM 2.0 v and PIDP profiles revealed specific patterns within the envelope glycoproteins (neuraminidase and hemagglutinin) of diverse strains of the H5N1 influenza virus. These patterns made it possible to identify structural and morphological similarities.

Conclusion: Using the PIM 2.0 v profile, our computational programs were able to identify the influenza H5N1 virus envelope glycoproteins (hemagglutinin and neuraminidase strains). This study contributes to a better comprehension of this emerging virus.

Keywords: Influenza H5N1 envelope glycoproteins, influenza H5N1 neuraminidase, influenza H5N1 hemagglutinin, intrinsic disorder predisposition, mutant proteins, polarity index method, polarity index method 2.0 v profile, structural proteomics.

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