Multienzyme degradation of host serum albumin in ticks

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00463315" target="_blank" >RIV/61388963:_____/16:00463315 - isvavai.cz</a>

Alternative codes found

RIV/60077344:_____/16:00463315 RIV/60076658:12310/16:43890858

Result on the web

<a href="http://dx.doi.org/10.1016/j.ttbdis.2015.12.014" target="_blank" >http://dx.doi.org/10.1016/j.ttbdis.2015.12.014</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ttbdis.2015.12.014" target="_blank" >10.1016/j.ttbdis.2015.12.014</a>

Result language

angličtina

Original language name

Multienzyme degradation of host serum albumin in ticks

Original language description

Host blood proteins, represented mainly by hemoglobin and serum albumin, serve as the ultimate source of amino acids needed for de novo protein synthesis during tick development and reproduction. While uptake and processing of hemoglobin by tick gut cells have been studied in detail, molecular mechanisms of host serum albumin degradation remain unknown. In this work, we have used artificial membrane feeding of Ixodes ricinus females on a hemoglobin-free diet in order to characterize the proteolytic machinery involved in albuminolysis. Morphological comparisons of ticks fed on whole blood (BF) and serum (SF) at microscopic and ultrastructural levels showed that albumin and hemoglobin have different trafficking routes in tick gut cells. Analysis in vitro with selective inhibitors demonstrated that albumin is degraded at an acidic pH by a network of cysteine and aspartic peptidases with predominant involvement of cysteine cathepsins having endo- and exopeptidase activities. The cleavage map of albumin and the roles of individual peptidases in albumin degradation were determined. These results indicate that the albuminolytic pathway is controlled by the same proteolytic system that is responsible for hemoglobinolysis. This was further supported by the overall similarity of gut peptidase profiles in SF and BF ticks at the transcriptional and enzymatic activity levels. In conclusion, our work provides evidence that although hemoglobin and albumin are transported differentially during heterophagy they are digested by a common multienzyme proteolytic network. This central digestive system, critical for successful blood feeding in tick females, thus represents a valuable target for novel anti-tick interventions.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

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

Name of the periodical

Ticks and Tick-borne Diseases

ISSN

1877-959X

e-ISSN

—

Volume of the periodical

7

Issue of the periodical within the volume

4

Country of publishing house

DE - GERMANY

Number of pages

10

Pages from-to

604-613

UT code for WoS article

000379279000008

EID of the result in the Scopus database

2-s2.0-84951806339