CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom

Montamas Suntravat; Paul R. Langlais; Elda E. Sánchez; Vance G. Nielsen

doi:10.1007/s10534-018-0107-5

CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom

Montamas Suntravat, Paul R. Langlais, Elda E. Sánchez, Vance G. Nielsen

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

It has been recently demonstrated that the hemotoxic venom activity of several species of snakes can be inhibited by carbon monoxide (CO) or a metheme forming agent. These and other data suggest that the biometal, heme, may be attached to venom enzymes and may be modulated by CO. A novel fibrinogenolytic metalloproteinase, named CatroxMP-II, was isolated and purified from the venom of a Crotalus atrox viper, and subjected to proteolysis and mass spectroscopy. An ion similar to the predicted singly charged m/z of heme at 617.18 was identified. Lastly, CORM-2 (tricarbonyldichlororuthenium (II) dimer, a CO releasing molecule) inhibited the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma. In conclusion, we present the first example of a snake venom metalloproteinase that is heme-bound and CO-inhibited.

Original language	English (US)
Pages (from-to)	585-593
Number of pages	9
Journal	Biometals
Volume	31
Issue number	4
DOIs	https://doi.org/10.1007/s10534-018-0107-5
State	Published - Aug 1 2018

Keywords

Carbon monoxide
Heme
Mass spectrometry
Snake venom metalloproteinase
Thrombelastography

ASJC Scopus subject areas

Biomaterials
General Biochemistry, Genetics and Molecular Biology
General Agricultural and Biological Sciences
Metals and Alloys

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10.1007/s10534-018-0107-5

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title = "CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom",

abstract = "It has been recently demonstrated that the hemotoxic venom activity of several species of snakes can be inhibited by carbon monoxide (CO) or a metheme forming agent. These and other data suggest that the biometal, heme, may be attached to venom enzymes and may be modulated by CO. A novel fibrinogenolytic metalloproteinase, named CatroxMP-II, was isolated and purified from the venom of a Crotalus atrox viper, and subjected to proteolysis and mass spectroscopy. An ion similar to the predicted singly charged m/z of heme at 617.18 was identified. Lastly, CORM-2 (tricarbonyldichlororuthenium (II) dimer, a CO releasing molecule) inhibited the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma. In conclusion, we present the first example of a snake venom metalloproteinase that is heme-bound and CO-inhibited.",

keywords = "Carbon monoxide, Heme, Mass spectrometry, Snake venom metalloproteinase, Thrombelastography",

author = "Montamas Suntravat and Langlais, {Paul R.} and S{\'a}nchez, {Elda E.} and Nielsen, {Vance G.}",

note = "Funding Information: Funding Funding for this project was provided by the NIH/ ORIP, Viper Resource Grant 5P40OD010960-14 (NNTRC, Texas A&M University-Kingsville, Dr. E.E. S{\'a}nchez) and NIH/ NHLBI Grant# 1R15HL137134-01 (Dr. M. Suntravat). Additional support was provided by the Robert A. Welch Foundation Department Grant, Grant number AC-0006 (TAMUK-Department of Chemistry). We would also like to thank, Nora Diaz DeLeon and Mark Hockm{\"u}ller (NNTRC Serpentarium curator) and all the NNTRC personnel. This investigation was also supported by the Departments of Medicine and Anesthesiology. Publisher Copyright: {\textcopyright} 2018, Springer Science+Business Media, LLC, part of Springer Nature.",

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AU - Langlais, Paul R.

AU - Sánchez, Elda E.

AU - Nielsen, Vance G.

N1 - Funding Information: Funding Funding for this project was provided by the NIH/ ORIP, Viper Resource Grant 5P40OD010960-14 (NNTRC, Texas A&M University-Kingsville, Dr. E.E. Sánchez) and NIH/ NHLBI Grant# 1R15HL137134-01 (Dr. M. Suntravat). Additional support was provided by the Robert A. Welch Foundation Department Grant, Grant number AC-0006 (TAMUK-Department of Chemistry). We would also like to thank, Nora Diaz DeLeon and Mark Hockmüller (NNTRC Serpentarium curator) and all the NNTRC personnel. This investigation was also supported by the Departments of Medicine and Anesthesiology. Publisher Copyright: © 2018, Springer Science+Business Media, LLC, part of Springer Nature.

PY - 2018/8/1

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N2 - It has been recently demonstrated that the hemotoxic venom activity of several species of snakes can be inhibited by carbon monoxide (CO) or a metheme forming agent. These and other data suggest that the biometal, heme, may be attached to venom enzymes and may be modulated by CO. A novel fibrinogenolytic metalloproteinase, named CatroxMP-II, was isolated and purified from the venom of a Crotalus atrox viper, and subjected to proteolysis and mass spectroscopy. An ion similar to the predicted singly charged m/z of heme at 617.18 was identified. Lastly, CORM-2 (tricarbonyldichlororuthenium (II) dimer, a CO releasing molecule) inhibited the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma. In conclusion, we present the first example of a snake venom metalloproteinase that is heme-bound and CO-inhibited.

AB - It has been recently demonstrated that the hemotoxic venom activity of several species of snakes can be inhibited by carbon monoxide (CO) or a metheme forming agent. These and other data suggest that the biometal, heme, may be attached to venom enzymes and may be modulated by CO. A novel fibrinogenolytic metalloproteinase, named CatroxMP-II, was isolated and purified from the venom of a Crotalus atrox viper, and subjected to proteolysis and mass spectroscopy. An ion similar to the predicted singly charged m/z of heme at 617.18 was identified. Lastly, CORM-2 (tricarbonyldichlororuthenium (II) dimer, a CO releasing molecule) inhibited the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma. In conclusion, we present the first example of a snake venom metalloproteinase that is heme-bound and CO-inhibited.

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CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom

Abstract

Keywords

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