DETERMINATION OF MUTATIONS IN THE GLYCOPROTEIN, VP24 AND VP40 PROTEINS IN THE MARBURG VIRUS AND INVESTIGATION IN SILICO OF THE INTERACTION OF THE GLYCOPROTEIN WITH ITS TAM FAMILY THAT CAUSES ITS INTRODUCTION TO THE HUMAN BODY

Öztürk S., Tarhan B., Aktaş E., Özdemir Özgentürk N.

ARCENG INTERNATIONAL SCIENTIFIC RESEARCH CONFERENCE, ASSIST. PROF. BURCU OZUBERK, Editör, ARCENG PUBLICATIONS,, Eskişehir, ss.11-22, 2024

  • Yayın Türü: Kitapta Bölüm / Araştırma Kitabı
  • Basım Tarihi: 2024
  • Yayınevi: ARCENG PUBLICATIONS,
  • Basıldığı Şehir: Eskişehir
  • Sayfa Sayıları: ss.11-22
  • Editörler: ASSIST. PROF. BURCU OZUBERK, Editör
  • Yıldız Teknik Üniversitesi Adresli: Evet

Özet

Millions of people lost their lives in the pandemic caused by SARS-COV, and therefore studies on viruses accelerated. One of the aims of our current study was to identify mutations in the Glycoprotein (surface protein) of Marburg virus, which may have pandemic potential according to the World Health Organization, and in the VP24 and VP40 proteins, which are critical for virion formation/release. Our other aim is to examine with in silico methods whether the mutations determined in the glycoprotein affect the interaction of the glycoprotein with TAM family receptors, which play a critical role in its entry into the host cell. Because Glycoprotein; Detailed bioinformatics analyzes of this protein may play a vital role in understanding the infection mechanism of the virus. Because this protein also serves as a critical component that directs the virus's ability to bind to target cells and enter the cell through this connection. as the ability to influence the immune system, possible approaches to modulate immune responses and develop treatment strategies. To emphasize, its glycoprotein stands out as an important component in understanding the biology and infection processes of Marburg virus. In this context, firstly, mutations of Glycoprotein, VP24 and VP40 proteins were detected using MEGAX. Mutations of the glycoprotein were examined with the Missence3D application and mutations affecting the structure were determined. TAM family receptors were rendered 3D using trRosetta and Phyre2 applications and brought into a format suitable for docking. Based on the three-dimensional structure of the normal and identified mutated glycoprotein, it was determined how possible mutations in the docking of TAM family receptors potentially affect this structure. It is thought that the results obtained will be an important resource not only for the Marburg virus, but also for research on the family members to which this virus belongs,such as the Ebola virus