Snake venom serine proteinases specificity mapping by proteomic identification of cleavage sites

Journal of Proteomics

Volumn 113, Issue , 2015, Pages 260-267

  Zelanis, André ^a,e   Huesgen, Pitter F ^b,c   Oliveira, Ana Karina ^a,d   Tashima, Alexandre K ^e   Serrano, Solange M T ^a   Overall, Christopher M ^b  

^a INSTITUTO BUTANTAN   (Brazil)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^c FORSCHUNGSZENTRUM JÜLICH   (Germany)

^d UNIVERSITY OF SÃO PAULO   (Brazil)

^e FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Peptide bond specificity; Proteome derived peptide library; Proteomic Identification of protease Cleavage Sites; Serine proteinase; Snake venom

Indexed keywords

SERINE PROTEINASE; SNAKE VENOM; BOTHROPS JARARACA PROTEASE A; PEPTIDE LIBRARY; THROMBOCYTE ACTIVATING FACTOR;

AMINO ACID SEQUENCE; ARTICLE; BOTHROPS JARARACA; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; LIQUID CHROMATOGRAPHY; NONHUMAN; PEPTIDE LIBRARY; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEOMIC IDENTIFICATION OF PROTEASE CLEAVAGE SITE; PROTEOMICS; SEQUENCE ALIGNMENT; TANDEM MASS SPECTROMETRY; ANIMAL; BOTHROPS; CHEMISTRY; ENZYMOLOGY; METABOLISM; PHYSIOLOGY;

ANIMALS; BOTHROPS; CROTALID VENOMS; PEPTIDE LIBRARY; PLATELET ACTIVATING FACTOR; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

EID: 84908529601     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.10.002     Document Type: Article

References (33)

1. Serrano S.M. The long road of research on snake venom serine proteinases. Toxicon 2013, 62:19-26.
2. Itoh N., Tanaka N., Funakoshi I., Kawasaki T., Mihashi S., Yamashina I. Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family. J Biol Chem 1988, 263:7628-7631.
3. Deshimaru M., Ogawa T., Nakashima K., Nobuhisa I., Chijiwa T., Shimohigashi Y., et al. M. Accelerated evolution of crotalinae snake venom gland serine proteases. FEBS Lett 1996, 397:83-88.
4. Parry M.A., Jacob U., Huber R., Wisner A., Bon C., Bode W. The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases. Structure 1998, 6:1195-1206.
5. Barrett A.J., Rawlings N.D. Families and clans of serine peptidases. Arch Biochem Biophys 1995, 318:247-250.
6. Kini R.M. The intriguing world of prothrombin activators from snake venom. Toxicon 2005, 45:1133-1145.
7. Serrano S.M., Maroun R. Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved. Toxicon 2005, 45:1115-1132.
8. Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C., Ho P.L., et al. Analysis of the ontogenetic variation in the venom proteome/peptidome of Bothrops jararaca reveals different strategies to deal with prey. J Proteome Res 2010, 9(5):2278-2291.
9. Zelanis A., Serrano S.M., Reinhold V.N. N-glycome profiling of Bothrops jararaca newborn and adult venoms. J Proteomics 2012, 75(3):774-782.
10. Mandelbaum F.R., Henriques O.B. Purification and properties of Bothrops protease A. Arch Biochem Biophys 1964, 104:369-374.
11. Mandelbaum F.R., Carrillo M., Henriques S.B. Proteolytic activity of Bothrops protease A on the B chain of oxidized insulin. Biochim Biophys Acta 1967, 132:508-510.
12. Reichl A.P., Assakura M.T., Mandelbaum F.R. Biophysical properties and amino acid composition of Bothrops protease A, a proteolytic enzyme isolated from the venom of the snake Bothrops jararaca (jararaca). Toxicon 1983, 21:421-427.
13. Murayama N., Saguchi K., Mentele R., Assakura M.T., Ohi H., Fujita Y., et al. The unusual high molecular mass of Bothrops protease A, a trypsin-like serine peptidase from the venom of Bothrops jararaca, is due to its high carbohydrate content. Biochim Biophys Acta 2003, 1652(1):1-6.
14. Paes Leme A.F., Prezoto B.C., Yamashiro E.T., Bertholim L., Tashima A.K., Klitzke C.F., et al. Bothrops protease A, a unique highly glycosylated serine proteinase, is a potent, specific fibrinogenolytic agent. J Thromb Haemost 2008, 6(8):1363-1372.
15. Serrano S.M., Mentele R., Sampaio C.A., Fink E. Purification, characterization, and amino acid sequence of a serine proteinase, PA-BJ, with platelet-aggregating activity from the venom of Bothrops jararaca. Biochemistry 1995, 34:7186-7193.
16. Santos B.F., Serrano S.M., Kuliopulos A., Niewiarowski S. Interaction of viper venom serine peptidases with thrombin receptors on human platelets. FEBS Lett 2000, 477:199-202.
17. Schilling O., Overall C.M. Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites. Nat Biotechnol 2008, 26(6):685-694.
18. Schilling O., Huesgen P.F., Barré O., Auf dem Keller U., Overall C.M. Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry. Nat Protoc 2011, 6(1):111-120.
19. Biniossek M.L., Nägler D.K., Becker-Pauly C., Schilling O. Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S. J Proteome Res 2011, 10(12):5363-5373.
20. Becker-Pauly C., Barré O., Schilling O., Auf dem Keller U., Ohler A., Broder C., et al. Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates. Mol Cell Proteomics 2011, 10(9). [M111.009233].
21. Paes Leme A.F., Escalante T., Pereira J.G., Oliveira A.K., Sanchez E.F., Gutiérrez J.M., et al. High resolution analysis of snake venom metalloproteinase (SVMP) peptide bond cleavage specificity using proteome based peptide libraries and mass spectrometry. J Proteomics 2011, 74(4):401-410.
22. Keller A., Eng J., Zhang N., Li X.J., Aebersold R. A uniform proteomics MS/MS analysis platform utilizing open XML file formats. Mol Syst Biol 2005, 1. [2005.0017].
23. Shteynberg D., Deutsch E.W., Lam H., Eng J.K., Sun Z., Tasman N., et al. iProphet: multi-level integrative analysis of shotgun proteomic data improves peptide and protein identification rates and error estimates. Mol Cell Proteomics 2011, 10(12). [M111.007690].
24. Vizcaíno J.A., Deutsch E.W., Wang R., Csordas A., Reisinger F., Ríos D., Dianes J.A., Sun Z., Farrah T., Bandeira N., Binz P.A., Xenarios I., Eisenacher M., Mayer G., Gatto L., Campos A., Chalkley R.J., Kraus H.J., Albar J.P., Martinez-Bartolomé S., Apweiler R., Omenn G.S., Martens L., Jones A.R., Hermjakob H. ProteomeXchange provides globally co-ordinated proteomics data submission and dissemination. Nat Biotechnol 2014, 30(3):223-226.
25. Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967, 27(2):157-162.
26. Colaert N., Helsens K., Martens L., Vandekerckhove J., Gevaert K. Improved visualization of protein consensus sequences by iceLogo. Nat Methods 2009, 6(11):786-787.
27. Evnin L.B., Vásquez J.R., Craik C.S. Substrate specificity of trypsin investigated by using a genetic selection. Proc Natl Acad Sci U S A 1990, 87(17):6659-6663.
28. Maroun R.C., Serrano S.M. Identification of the substrate-binding exosites of two snake venom serine proteinases: molecular basis for the partition of two essential functions of thrombin. J Mol Recognit 2004, 17(1):51-61.
29. Markland F.S. Snake venoms and the hemostatic system. Toxicon 1998, 36:1749-1800.
30. Pirkle H. Thrombin-like enzymes from snake venoms: an updated inventory. Thromb Haemost 1998, 79:675-683.
31. Braud S., Parry M.A., Maroun R., Bon C., Wisner A. The contribution of residues 192 and 193 to the specificity of snake venom serine proteinases. J Biol Chem 2000, 275:1823-1828.
32. Maroun R.C. Molecular basis for the partition of the essential functions of thrombin among snake venom serine proteinases: the case of thrombin-like enzymes. Haemostasis 2001, 31:247-256.
33. Fox J.W., Serrano S.M. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J 2008, 275(12):3016-3030.