Deciphering foot-and-mouth disease (FMD) virus–host tropism. Issue 18 (12th December 2019)

• Record Type: Journal Article
• Authors: Singh, Indra; Deb, Rajib; Kumar, Sanjeev; Singh, Rani; Andonissamy, Jerome; Smita, Shuchi; Sengar, Gyanendra Singh; Kumar, Rajiv; Ojha, Krishna Kumar; Sahoo, Nihar Ranjan; Murali, S; Chandran, Rejani; Nair, Radhakrishnan V; Lal, S B; Mishra, Dwijesh Chandra; Rai, Anil
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 37:Issue 18(2019)
• Page Start: 4779
• Page End: 4789
• Publication Date: 2019-12-12
• Subjects: Foot-and-mouth disease (FMD) -- integrin -- interaction -- KR779877 -- tropism; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2019.1567386
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract: The pattern of interactions between foot and mouth disease (FMD) viral protein 1 (VP1) with susceptible and resistant host integrins were deciphered. The putative effect of site-directed mutation on alteration of interaction is illustrated using predicted and validated 3D structures of VP1, mutated VP1 and integrins of Bos taurus, Gallus and Canis . Strong interactions were observed between FMDV-VP1 protein motifs at conserved tripeptide, Arg-Gly-Asp 143 RGD 145 and at domain 676 SIPLQ 680 in alpha-integrin of B. taurus. Notably, in-silico site-directed mutation in FMDV-VP1 protein led to complete loss of interaction between FMD-VP1 protein and B. taurus integrin, which confirmed the active role of arginine-glycine-aspartic acid (RGD) domain. Interestingly, in-vitro analysis demonstrates the persistence of the putative tropism site 'SIPLQ' in different cattle breeds undertaken. Thus, the attempt to decipher the tropism of FMDV at host receptor level interaction might be useful for future FMD control strategies through development of mimetic marker vaccines and/or host receptor manipulations. Communicated by Ramaswamy H. Sarma