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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Bothrops jararaca accessory venom gland is an ancillary source of toxins to the snake

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Author(s):
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Valente, Richard Hemmi [1, 2] ; Luna, Milene Schmidt [3] ; de Oliveira, Ursula Castro [4] ; Nishiyama-Junior, Milton Yutaka [4] ; Junqueira-de-Azevedo, Inacio de Loiola [4] ; Portes-Junior, Jose Antonio [5] ; Clissa, Patricia Bianca [5] ; Viana, Luciana Godoy [3] ; Sanches, Leonardo [6] ; Moura-da-Silva, Ana Maria [5, 6] ; Perales, Jonas [1, 2] ; Yamanouye, Norma [3, 2]
Total Authors: 12
Affiliation:
[1] Fiocruz MS, Lab Toxinol, Inst Oswaldo Cruz, Ave Brasil 4365, BR-21040900 Rio De Janeiro - Brazil
[2] CNPq, Inst Nacl Ciencia & Tecnol Toxinas INCTTox, Brasilia, DF - Brazil
[3] Inst Butantan, Lab Farmacol, Ave Vital Brazil 1500, BR-05503900 Sao Paulo - Brazil
[4] Inst Butantan, Lab Especial Toxinol Aplicada, CeTICS, Ave Vital Brazil 1500, BR-05503900 Sao Paulo - Brazil
[5] Inst Butantan, Lab Imunopatol, Ave Vital Brazil 1500, BR-05503900 Sao Paulo - Brazil
[6] Inst Butantan, Lab Ecol & Evolucao, Ave Vital Brazil 1500, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 6
Document type: Journal article
Source: JOURNAL OF PROTEOMICS; v. 177, p. 137-147, APR 15 2018.
Web of Science Citations: 0
Abstract

In Viperidae snakes, it has been attributed to the main venom gland, a component of the venom gland apparatus, the function of synthesizing all venom toxins and storing them inside a basal-central lumen. However, the role of the accessory gland is still unknown. Here, we analyzed the proteome and the transcriptome of the accessory gland during venom production and secretion cycle. We showed that the accessory gland expresses and synthesizes toxins that are similar to those produced by the main venom gland such as C-type lectin/C-type lectin-like proteins, metalloproteinase, phospholipase A(2), cysteine rich secretory protein, nerve growth factor, vascular endothelial growth factor, serine proteinase, and L-amino acid oxidase. Our data have shown that toxin synthesis in the accessory gland is asynchronous when compared to the same process in the venom gland. Moreover, this gland also expresses inhibitors of venom phospholipases A(2) and metalloproteinases. Transcriptome analysis showed that the transcripts that correspond to toxins in the accessory gland have a good correlation to the main venom gland transcripts. Therefore, it is proposed that the accessory gland is an ancillary source of toxins to the snake, and provides inhibitors that could control venom toxicity (and integrity) during storage. Significance: In this study, we propose that the accessory venom gland acts as an important ancillary source of toxins to the snake, in lieu of a depleted main venom gland, and provides inhibiting agents that control venom toxicity (and integrity) during its storage. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 16/50127-5 - Dimensions US-BIOTA São Paulo: scales of biodiversity: integrated studies of snake venom evolution and function across multiple levels of diversity
Grantee:Inácio de Loiola Meirelles Junqueira de Azevedo
Support type: BIOTA-FAPESP Program - Thematic Grants
FAPESP's process: 14/26058-8 - Inhibition of mammalian and snake venom metalloproteinases by the recombinant pro-domain of jararhagin and its relevant peptide fragments
Grantee:Ana Maria Moura da Silva
Support type: Regular Research Grants