Journal Article

Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom

Vasaruchapong, Taksa, Chaiyabutr, Narongsak, Khow, Orawan, Reamtong, Onrapak, Thiangtrongjit, Tipparat, Laoungbua, Panithi, Noiphrom, Jureeporn, Tubtimyoy, Arissara, Sitprija, Siravit, Kumkate, Supeecha, Chanhome, Lawan

2021

Overview

The venomic profile of Asian mountain pit viper Ovophis monticola is clarified in the present study. Using mass spectrometry-based proteomics, 247 different proteins were identified in crude venom of O . monticola found in Thailand. The most abundant proteins were snake venom metalloproteases (SVMP) (36.8%), snake venom serine proteases (SVSP) (31.1%), and phospholipases A 2 (PLA 2 ) (12.1%). Less abundant proteins included L-amino acid oxidase (LAAO) (5.7%), venom nerve growth factor (3.6%), nucleic acid degrading enzymes (3.2%), C-type lectins (CTL) (1.6%), cysteine-rich secretory proteins (CRISP) (1.2%) and disintegrin (1.2%). The immunoreactivity of this viper’s venom to a monovalent antivenom against green pit viper Trimeresurus albolabris , or to a polyvalent antivenom against hemotoxic venom was investigated by indirect ELISA and two-dimensional (2D) immunoblotting. Polyvalent antivenom showed substantially greater reactivity levels than monovalent antivenom. A titer for the monovalent antivenom was over 1:1.28x10 7 dilution while that of polyvalent antivenom was 1:5.12x10 7 . Of a total of 89 spots comprising 173 proteins, 40 spots of predominantly SVMP, SVSP and PLA 2 were specific antigens for antivenoms. The 49 unrecognized spots containing 72 proteins were characterized as non-reactive proteins, and included certain types of CTLs and CRISPs. These neglected venom constituents could limit the effectiveness of antivenom-based therapy currently available for victims of pit viper envenomation.

• Publisher: Public Library of Science,Public Library of Science (PLoS)
• Subject: Amino acid oxidase / Amino acids / Animals / Antigens / Antivenins / Antivenom / Biology / Biology and Life Sciences / Cytotoxicity / Dilution / Disintegrins - chemistry / Enzyme-linked immunosorbent assay / Growth factors / Immunoblotting / Immunoreactivity / L-Amino Acid Oxidase - chemistry / Lectins / Lectins, C-Type - chemistry / Lymphocytes T / Mass Spectrometry / Mass spectroscopy / Medical research / Medicine / Medicine and Health Sciences / Medicine, Experimental / Metalloproteases - chemistry / Mountains / Nerve growth factor / Nerve Growth Factor - chemistry / Nucleic acids / Ovophis monticola / Peptides / Phospholipase A2 / Phospholipases A2 - chemistry / Physical Sciences / Proteins / Proteome - chemistry / Proteomics / R&D / Research & development / Serine Proteases - chemistry / Serine proteinase / Snack foods / Snakes / Thailand / Trimeresurus / Venom