Carlos Polanco, Alberto Huberman, Vladimir N. Uversky, Martha Rios Castro, Brayans Becerra-Luna, Enrique Hernandez Lemus, Claudia Pimentel-Hernández, Mireya Martínez-Garcia, Thomas Buhse, Cynthia Karen Gutierrez Juárez, Gilberto Vargas Alarcon, Gabriela Calvo-Leroux Corona, Francisco J. Roldan Gomez, Juan Luciano Díaz-González, Raul Martinez-Memije, Pedro L. Flores Ch
{"title":"Computational Analysis of Marburg Virus Envelope Glycoproteins: Insights from Bioinformatics and Genomics","authors":"Carlos Polanco, Alberto Huberman, Vladimir N. Uversky, Martha Rios Castro, Brayans Becerra-Luna, Enrique Hernandez Lemus, Claudia Pimentel-Hernández, Mireya Martínez-Garcia, Thomas Buhse, Cynthia Karen Gutierrez Juárez, Gilberto Vargas Alarcon, Gabriela Calvo-Leroux Corona, Francisco J. Roldan Gomez, Juan Luciano Díaz-González, Raul Martinez-Memije, Pedro L. Flores Ch","doi":"10.2174/0115734110298101240629090801","DOIUrl":null,"url":null,"abstract":"Background: Marburg virus (MARV), which is spread by one species of fruit bats, can cause deadly Marburg virus disease (MVD, also known as Marburg hemorrhagic fever, MHF), which is a severe form of viral hemorrhagic fever with symptoms similar to Ebola. MARV is considered to be very dangerous, and there are no approved vaccines or antiviral treatments for Marburg disease. Objective: Computational studies were conducted to comprehend the envelope glycoproteins GP1 and GP2 expressed by the Marburg virus. Methods: Determination of the predicted intrinsic disorder predisposition of each glycoprotein sequence (PIDP) and the Polarity Index Method Profile 3.0v (PIM 3.0v) using genomics software and multiple computer algorithms, several of which have been specifically designed for this purpose. Results: The PIM 3.0v and PIDP profiles showed different MARV envelope glycoprotein patterns. These patterns revealed structural and morphological commonalities. Conclusions: Our computer systems were able to identify MARV envelope glycoprotein isolates using the PIM 3.0v profile, and they suggest that they can be used as a first-step filter for identifying them from databases or building synthetic proteins.","PeriodicalId":10742,"journal":{"name":"Current Analytical Chemistry","volume":"43 1","pages":""},"PeriodicalIF":1.7000,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Analytical Chemistry","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.2174/0115734110298101240629090801","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, ANALYTICAL","Score":null,"Total":0}
引用次数: 0
Abstract
Background: Marburg virus (MARV), which is spread by one species of fruit bats, can cause deadly Marburg virus disease (MVD, also known as Marburg hemorrhagic fever, MHF), which is a severe form of viral hemorrhagic fever with symptoms similar to Ebola. MARV is considered to be very dangerous, and there are no approved vaccines or antiviral treatments for Marburg disease. Objective: Computational studies were conducted to comprehend the envelope glycoproteins GP1 and GP2 expressed by the Marburg virus. Methods: Determination of the predicted intrinsic disorder predisposition of each glycoprotein sequence (PIDP) and the Polarity Index Method Profile 3.0v (PIM 3.0v) using genomics software and multiple computer algorithms, several of which have been specifically designed for this purpose. Results: The PIM 3.0v and PIDP profiles showed different MARV envelope glycoprotein patterns. These patterns revealed structural and morphological commonalities. Conclusions: Our computer systems were able to identify MARV envelope glycoprotein isolates using the PIM 3.0v profile, and they suggest that they can be used as a first-step filter for identifying them from databases or building synthetic proteins.
期刊介绍:
Current Analytical Chemistry publishes full-length/mini reviews and original research articles on the most recent advances in analytical chemistry. All aspects of the field are represented, including analytical methodology, techniques, and instrumentation in both fundamental and applied research topics of interest to the broad readership of the journal. Current Analytical Chemistry strives to serve as an authoritative source of information in analytical chemistry and in related applications such as biochemical analysis, pharmaceutical research, quantitative biological imaging, novel sensors, and nanotechnology.