Quantitative assessment of Newcastle disease virus proteins interactions with all known mucin types of Chicken and Quail

Author:

Almhanna Hazem,Kumar Arun HSORCID

Abstract

AbstractBackgroundNewcastle Disease (ND), caused by the Newcastle Disease Virus (NDV) poses a significant threat to poultry, leading to severe economic losses. Understanding the molecular interactions between NDV proteins and avian mucins is crucial for developing targeted interventions.Material and MethodsIn this study, twelve NDV proteins were systematically assessed for their interactions with sixteen quail and eight chicken mucin types, revealing diverse and species-specific binding patterns.ResultsHigh-affinity interactions between mucins (Muc5A, Muc5B, and Muc6) and NDV hemagglutinin-neuraminidase, was observed in addition to significant interactions with NDV fusion glycoprotein. Notably, chicken Muc4 displayed mid-range interactions exclusively with NDV fusion glycoprotein, highlighting potential species-specific differences in viral entry mechanisms between quails and chickens. Furthermore, the study investigated the number of binding sites on NDV proteins and chicken/quail mucins. Chicken Muc5B emerged as a standout with the highest number (20) of binding sites, suggesting its crucial role in NDV infection. The binding site analysis identified key regions in NDV fusion glycoprotein and hemagglutinin-neuraminidase, indicating potential targets for vaccine development.ConclusionThis study provides a foundation for future research into optimizing diagnostic approaches and therapeutic strategies for NDV infections. Validation of these interactions with real-world clinical data, coupled with an exploration of tissue-specific mucin expression patterns, could further enhance our understanding of host-virus dynamics. The identified interactions offer promising avenues for developing vaccines that target specific binding sites, thereby contributing to the effective control and prevention of Newcastle Disease in poultry populations.

Publisher

Cold Spring Harbor Laboratory

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