Dynamic secretome of Trichomonas vaginalis: Case study of beta-amylases

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F18%3A00508052" target="_blank" >RIV/86652036:_____/18:00508052 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/18:10376224

Result on the web

<a href="https://www.mcponline.org/content/17/2/304" target="_blank" >https://www.mcponline.org/content/17/2/304</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/mcp.RA117.000434" target="_blank" >10.1074/mcp.RA117.000434</a>

Result language

angličtina

Original language name

Dynamic secretome of Trichomonas vaginalis: Case study of beta-amylases

Original language description

The secretion of virulence factors by parasitic protists into the host environment plays a fundamental role in multifactorial host-parasite interactions. Several effector proteins are known to be secreted by Trichomonas vaginalis, a human parasite of the urogenital tract. However, a comprehensive profiling of the T. vaginalis secretome remains elusive, as do the mechanisms of protein secretion. In this study, we used high-resolution label-free quantitative MS to analyze the T. vaginalis secretome, considering that secretion is a time- and temperature-dependent process, to define the cutoff for secreted proteins. In total, we identified 2 072 extracellular proteins, 89 of which displayed significant quantitative increases over time at 37 degrees C. These 89 bona fide secreted proteins were sorted into 13 functional categories. Approximately half of the secreted proteins were predicted to possess transmembrane helixes. These proteins mainly include putative adhesins and leishmaniolysin-like metallopeptidases. The other half of the soluble proteins include several novel potential virulence factors, such as DNaseII, pore-forming proteins, and beta-amylases. Interestingly, current bioinformatic tools predicted the secretory signal in only 18% of the identified T. vaginalis-secreted proteins. Therefore, we used beta-amylases as a model to investigate the T. vaginalis secretory pathway. We demonstrated that two beta-amylases( BA1 and BA2) are transported via the classical endoplasmic reticulum-to-Golgi pathways, and in the case of BA1, we showed that the protein is glycosylated with multiple N-linked glycans of Hex(5)HexNAc(2) structure. The secretion was inhibited by brefeldin A but not by FLI-06. Another two beta-amylases (BA3 and BA4), which are encoded in the T. vaginalis genome but absent from the secretome, were targeted to the lysosomal compartment. Collectively, under defined in vitro conditions, our analysis provides a comprehensive set of constitutively secreted proteins that can serve as a reference for future comparative studies, and it provides the first information about the classical secretory pathway in this parasite.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

<a href="/en/project/ED1.1.00%2F02.0109" target="_blank" >ED1.1.00/02.0109: Biotechnology and Biomedicine Centre of the Academy of Sciences and Charles University</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Molecular and Cellular Proteomics

ISSN

1535-9476

e-ISSN

—

Volume of the periodical

17

Issue of the periodical within the volume

2

Country of publishing house

US - UNITED STATES

Number of pages

17

Pages from-to

304-320

UT code for WoS article

000424091400008

EID of the result in the Scopus database

2-s2.0-85041736778