title: Interrogating the Venom of the Viperid Snake Sistrurus catenatus edwardsii by a Combined Approach of Electrospray and MALDI Mass Spectrometry.
abstract: The complete sequence characterization of snake venom proteins by mass spectrometry is rather challenging due to the presence of multiple isoforms from different protein families. In the present study, we investigated the tryptic digest of the venom of the viperid snake Sistrurus catenatus edwardsii by a combined approach of liquid chromatography coupled to either electrospray (online) or MALDI (offline) mass spectrometry. These different ionization techniques proved to be complementary allowing the identification a great variety of isoforms of diverse snake venom protein families, as evidenced by the detection of the corresponding unique peptides. For example, ten out of eleven predicted isoforms of serine proteinases of the venom of S. c. edwardsii were distinguished using this approach. Moreover, snake venom protein families not encountered in a previous transcriptome study of the venom gland of this snake were identified. In essence, our results support the notion that complementary ionization techniques of mass spectrometry allow for the detection of even subtle sequence differences of snake venom proteins, which is fundamental for future structure-function relationship and possible drug design studies.
authors.affiliation: Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, RJ, 21045-900, Brazil; Department of Biological Sciences, 14 Science Drive 4, National University of Singapore, Singapore, 117543, Singapore.
authors.forename: Alex
authors.initials: A
authors.lastname: Chapeaurouge
authors.affiliation: Department of Biological Sciences, 14 Science Drive 4, National University of Singapore, Singapore, 117543, Singapore.
authors.forename: Md Abu
authors.initials: MA
authors.lastname: Reza
authors.affiliation: School of Biological Sciences, University of Northern Colorado, 501 20th St., CB 92, Greeley, Colorado, 80639-0017, United States of America.
authors.forename: Stephen P
authors.initials: SP
authors.lastname: Mackessy
authors.affiliation: Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, RJ, 21045-900, Brazil; Laboratory for Proteomics and Protein Engineering, Carlos Chagas Institute, Fiocruz, Curitiba, PR, 81350-010, Brazil.
authors.forename: Paulo C
authors.initials: PC
authors.lastname: Carvalho
authors.affiliation: Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, RJ, 21045-900, Brazil.
authors.forename: Richard H
authors.initials: RH
authors.lastname: Valente
authors.affiliation: Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, RJ, 21045-900, Brazil.
authors.forename: André
authors.initials: A
authors.lastname: Teixeira-Ferreira
authors.affiliation: Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, RJ, 21045-900, Brazil.
authors.forename: Jonas
authors.initials: J
authors.lastname: Perales
authors.affiliation: Department of Biological Sciences, 14 Science Drive 4, National University of Singapore, Singapore, 117543, Singapore.
authors.forename: Qingsong
authors.initials: Q
authors.lastname: Lin
authors.affiliation: Department of Biological Sciences, 14 Science Drive 4, National University of Singapore, Singapore, 117543, Singapore; Department of Biochemistry and Molecular Biology, Medical College of Virginia, Virginia Commonwealth University, Richmond, Virginia, 23298-0614, United States of America.
authors.forename: R Manjunatha
authors.initials: RM
authors.lastname: Kini
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008666:Metalloendopeptidases / Q000032:analysis; D008969:Molecular Sequence Data; D040901:Proteomics / Q000379:methods; D030162:Reptilian Proteins / Q000032:analysis*; D016415:Sequence Alignment; D057057:Serine Proteases / Q000032:analysis; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D014757:Viper Venoms / Q000737:chemistry*; D017819:Viperidae / Q000378:metabolism
chemical_list: D030162:Reptilian Proteins; D014757:Viper Venoms; D057057:Serine Proteases; D008666:Metalloendopeptidases