SLAM (CD150) receptor homologous peptides block the peste des petits ruminants virus entry into B95a cells

Author:

Agrawal Aditya12ORCID,Varshney Rajat34,Gattani Anil15,Kirthika Perumalraja16,Gupta Rohini7,Kumar Deepak8,Singh Rabindra Prasad9,Singh Praveen110

Affiliation:

1. Division of Biochemistry ICAR‐IVRI Bareilly Uttar Pradesh India

2. Department of Veterinary Physiology and Biochemistry College of Veterinary Science and Animal Husbandry Rewa Madhya Pradesh India

3. Department of Veterinary Microbiology, Faculty of Veterinary and Animal Sciences, Rajiv Gandhi South Campus Banaras Hindu University Mirzapur Uttar Pradesh India

4. Division of Bacteriology and Mycology ICAR‐IVRI Bareilly Uttar Pradesh India

5. Department of Veterinary Biochemistry NDVSU Jabalpur Madhya Pradesh India

6. Department of Biochemistry and Molecular Biology Mayo Clinic Rochester Minnesota USA

7. Department of Veterinary Medicine NDVSU Jabalpur Madhya Pradesh India

8. Division of Veterinary Biotechnology ICAR‐IVRI Bareilly Uttar Pradesh India

9. Division of Biological Products ICAR‐IVRI Bareilly Uttar Pradesh India

10. Biophysics Section ICAR‐IVRI Bareilly Uttar Pradesh India

Abstract

AbstractThe fusion of haemagglutinin‐neuraminidase (HN) protein of peste des petits ruminant (PPR) virus with signaling lymphocyte activation molecules (SLAM) host cell receptor consequences the virus entry and multiplication inside the host cell. The use of synthetic SLAM homologous peptides (i.e., molecular decoy for HN protein of PPR virus) may check PPR infection at the preliminary stage. Hence, the predicted SLAM homologous peptides using bioinformatics tools were synthesized by solid phase chemistry with standard Merrifield's 9‐fluorenylmethoxycarbonyl (Fmoc) chemistry and were purified by reverse phase high performance liquid chromatography. The secondary structures of synthesized peptides were elucidated by circular dichroism spectroscopy. The in vitro interactions of these peptides were studied through indirect Enzyme Linked Immuno Sorbent Assay (ELISA) and visual surface plasmon UV‐visible spectroscopy. The SLAM homologous peptides were able to interact with the peste des petits ruminant virus (PPRV) with varying binding efficiency. The interaction of SLAM homologous peptide with the PPR virus was ascertained by the change in the plasmon color from red wine to purple during visual detection and also by bathochromic shift in absorbance spectra under UV‐visible spectrophotometry. The cytotoxic and anti‐PPRV effect of these peptides were also evaluated in B95a cell line using PPR virus (Sungri/96). The cytotoxic concentration 50 (CC50) value of each peptide was greater than 1000 μg mL−1. The anti‐PPRV efficiency of SLAM‐22 was relatively high among SLAM homologous peptides, SLAM‐22 at 25 μg mL−1 concentration showed a reduction of more than log10 3 virus titer by priming of B95a cell line while the use of SLAM‐15 and Muco‐17 at the same concentration dropped virus titer from log10 4.8 to log10 2.5 and log10 3.1 respectively. The concentration of SLAM homologous peptide (25 μg mL−1) to exert its anti‐PPRV effect was much less than its CC50 level (>1000 μg mL−1). Therefore, the synthetic SLAM homologous peptides may prove to be better agents to target PPRV.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

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