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Identification, description and structural analysis of beta phospholipase A2 inhibitors (sb?PLIs) from Latin American pit vipers indicate a binding site region for basic snake venom phospholipases A2.

ABSTRACT: Several snake species possess, in their circulating blood, endogenous PLA2 inhibitors (sbPLIs) with the primary function of natural protection against toxic enzymes from homologous and heterologous venoms. Among the three structural classes of sbPLIs - named ?, ?, and ? - the ? class (sb?PLIs) is the least known with only four identified sequences, so far. The last class of inhibitors encompass molecules with leucine rich repeats (LRRs) motifs containing repeating amino acid segments. In the present study, we identified and characterized putative sb?PLIs from the liver and venom glands of six Latin American pit vipers belonging to Bothrops and Crotalus genera. The inhibitor from Crotalus durissus terrificus snakes (Cdtsb?PLI) was chosen as a reference for the construction of the first in silico structural model for this class of inhibitors, using molecular modeling and molecular dynamics simulations. Detailed analyses of the electrostatic surface of the Cdtsb?PLI model and protein-protein docking with crotoxin B from homologous venoms predict the interacting surface between these proteins.

SUBMITTER: Fortes-Dias CL

PROVIDER: S-EPMC7286088 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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Identification, description and structural analysis of beta phospholipase A2 inhibitors (sbβPLIs) from Latin American pit vipers indicate a binding site region for basic snake venom phospholipases A2.

Fortes-Dias Consuelo Latorre CL Fernandes Carlos Alexandre H CAH Ortolani Paula Ladeira PL Campos Patrícia Cota PC Melo L A LA Felicori Liza Figueiredo LF Fontes Marcos Roberto M MRM

Toxicon: X 20190226

Several snake species possess, in their circulating blood, endogenous PLA2 inhibitors (sbPLIs) with the primary function of natural protection against toxic enzymes from homologous and heterologous venoms. Among the three structural classes of sbPLIs - named α, β, and γ - the β class (sbβPLIs) is the least known with only four identified sequences, so far. The last class of inhibitors encompass molecules with leucine rich repeats (LRRs) motifs containing repeating amino acid segments. ...[more]

PMID: 32550566

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Project description:We report a genus-wide comparison of venom proteome variation across New World pit vipers in the genus Agkistrodon. Despite the wide variety of habitats occupied by this genus and that all its taxa feed on diverse species of vertebrates and invertebrate prey, the venom proteomes of copperheads, cottonmouths, and cantils are remarkably similar, both in the type and relative abundance of their different toxin families. The venoms from all the eleven species and subspecies sampled showed relatively similar proteolytic and PLA2 activities. In contrast, quantitative differences were observed in hemorrhagic and myotoxic activities in mice. The highest myotoxic activity was observed with the venoms of A. b. bilineatus, followed by A. p. piscivorus, whereas the venoms of A. c. contortrix and A. p. leucostoma induced the lowest myotoxic activity. The venoms of Agkistrodon bilineatus subspecies showed the highest hemorrhagic activity and A. c. contortrix the lowest. Compositional and toxicological analyses agree with clinical observations of envenomations by Agkistrodon in the USA and Central America. A comparative analysis of Agkistrodon shows that venom divergence tracks phylogeny of this genus to a greater extent than in Sistrurus rattlesnakes, suggesting that the distinct natural histories of Agkistrodon and Sistrurus clades may have played a key role in molding the patterns of evolution of their venom protein genes.Biological significanceA deep understanding of the structural and functional profiles of venoms and of the principles governing the evolution of venomous systems is a goal of venomics. Isolated proteomics analyses have been conducted on venoms from many species of vipers and pit vipers. However, making sense of these large inventories of data requires the integration of this information across multiple species to identify evolutionary and ecological trends. Our genus-wide venomics study provides a comprehensive overview of the toxic arsenal across Agkistrodon and a ground for understanding the natural histories of, and clinical observations of envenomations by, species of this genus.

Dataset Information

Identification, description and structural analysis of beta phospholipase A2 inhibitors (sb?PLIs) from Latin American pit vipers indicate a binding site region for basic snake venom phospholipases A2.

Publications

Identification, description and structural analysis of beta phospholipase A<sub>2</sub> inhibitors (sbβPLIs) from Latin American pit vipers indicate a binding site region for basic snake venom phospholipases A<sub>2</sub>.

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