Proteomics

Dataset Information

0

Triatoma sordida salivary glands LC-MSMS


ABSTRACT: Triatoma sordida salivary glands secrete a number of complex bioactive proteins during feeding that affect hemostatic and immunological systems from vertebrate hosts. In this study, salivary glands and saliva were collected from 5th instar nymphs and adult triatomines. Liquid chromatography tandem-mass spectrometry (LC-MS/MS) was used to identify T. sordida salivary proteins. A total of 133 proteins was identified. Lipocalins, Hemiptera specific families, CRiSP/Antigen-5 and Kazal-type protein inhibitors proteins match to 42.01%, 14.32%, 5.86% and 1.91% of the total spectrum count, respectively. These proteins are involved in several physiological roles, including anti-coagulant, immunity and anti-microorganism. Salivary proteins contribute to successful feeding.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Triatoma Sordida

TISSUE(S): Saliva

SUBMITTER: Carla Araújo  

LAB HEAD: Sèbastien Olivier Charneau

PROVIDER: PXD028350 | Pride | 2022-02-15

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Ts_Replicate1.raw Raw
Ts_Replicate1.sqt Other
Ts_Replicate2.raw Raw
Ts_Replicate2.sqt Other
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Publications


Triatomines have evolved salivary glands that produce versatile molecules with various biological functions, including those leading their interactions with vertebrate hosts' hemostatic and immunological systems. Here, using high-throughput transcriptomics and proteomics, we report the first sialome study on the synanthropic triatomine <i>Triatoma sordida</i>. As a result, 57,645,372 reads were assembled into 26,670 coding sequences (CDS). From these, a total of 16,683 were successfully annotate  ...[more]

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