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Deciphering foot-and-mouth disease (FMD) virus–host tropism

Version 3 2019-09-17, 11:44
Version 2 2019-02-07, 12:47
Version 1 2019-01-18, 09:16
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posted on 2019-02-07, 12:47 authored by Indra Singh, Rajib Deb, Sanjeev Kumar, Rani Singh, Jerome Andonissamy, Shuchi Smita, Gyanendra Singh Sengar, Rajiv Kumar, Krishna Kumar Ojha, Nihar Ranjan Sahoo, S Murali, Rejani Chandran, Radhakrishnan V Nair, S B Lal, Dwijesh Chandra Mishra, Anil Rai

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 143RGD145 and at domain 676SIPLQ680 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

Funding

This work was supported by MeitY and DST, Govt. of India at CABin, ICAR-IASRI, New Delhi and at ICAR-CIRC, Meerut for in-vivo and in-vitro work, respectively [grant number HPC projects/2(1)/2012], [grant number SR/WOS-A/LS-437/2012(G)].

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