mass-spectrometry-congress-2019-posters-abstracts

Page 50

May 20-21, 2019 | Rome, Italy

OF EXCELLENCE

IN INTERNATIONAL

MEETINGS

YEARS

Journal of Chemical Technology and Applications | Volume 3

MASS SPECTROMETRY,

PROTEOMICS AND POLYMER CHEMISTRY

International Conference on

Mass Spectrometry Congress 2019

PROTEOMIC PROFILE, BIOLOGICAL ACTIVITIES AND ANTIGENIC ANALYSIS OF THE

VENOM FROM BOTHRIOPSIS BILINEATA SMARAGDINA (“LORO MACHACO”), A PIT VI-

PER SNAKE FROM PERU

Carolina Rego Rodrigues

Universidade Federal de Minas Gerais (UFMG), Brazil

n Peru, snakebite is a public health problem, especially in the rain forest, as a result of progressive colonization

of this geographical area. This country is the second in Latin America, after Brazil, to exhibit the largest variety

of venomous snakes. B. atrox and B. b. smaragdina snakes are sympatric species in Peruvian Amazon region

and are responsible for approximately 95% of the envenomings reported in this region. B. b. smaragdina may

cause a smaller share (3 to 38%) of those accidents, due to its arboreal habits, that make human encounters

with these snakes less likely to happen. Despite B. b. smaragdina recognized medical importance, its venom

composition and biological activities have been poorly studied. In order to determine Bothriopsis bilineata

smaragdina venom (BbsV) composition, proteomic approaches were performed. Venom components were

analyzed by RP-HPLC, SDS-PAGE and nano LC on line with LTQ Orbitrap XL. Results showed a total of 189 iden-

tified proteins, grouped into 11 different subgroups which include snake venom metalloproteinases (SVMPs,

54.67%), snake C-type lectins (Snaclecs, 15.78%), snake venom serine proteinases (SVSPs, 14.69%), cystein-rich

secretory proteins (CRISP, 2.61%), phospholipases A2 (PLA2, 1.14%), phosphodiesterase (PDE, 1.17%), venom

endothelial growth factor (VEGF, 1.06%) 5’nucleotidases (0.33%), L-amino acid oxidases (LAAOs, 0.28%) and

other proteins.

In vitro

enzymatic activities (SVMP, SVSP, LAAO, Hyal and PLA2) of BbsV were also analyzed.

BbsV showed high SVSP activity but low PLA2 activity, when compared to other Bothrops venoms.

In vivo

BbsV induced haemorrhage and edema in mice and showed intraperitoneal median lethal dose (LD50); 92.74

(± 0.15) μg/20 g of mice. Furthermore, BbsV reduced cell viability when incubated with VERO cells. Peruvian

and Brazilian bothropic antivenoms recognize BbsV proteins, as detected by ELISA and Western Blotting. Both

antivenoms were able to neutralize

in vivo

edema and haemorrhage.

J Chem Tech App 2019, Volume 3