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Tryptogalinin Is a Tick Kunitz Serine Protease Inhibitor with a Unique Intrinsic Disorder
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SYSNO ASEP 0397485 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Tryptogalinin Is a Tick Kunitz Serine Protease Inhibitor with a Unique Intrinsic Disorder Tvůrce(i) Valdés, James J. (BC-A) RID, ORCID
Schwarz, Alexandra (BC-A)
Cabeza de Vaca, I. (ES)
Calvo, E. (US)
Pedra, J. H. F. (US)
Guallar, V. (ES)
Kotsyfakis, Michalis (BC-A) RID, ORCIDZdroj.dok. PLoS ONE. - : Public Library of Science - ISSN 1932-6203
Roč. 8, č. 5 (2013), e62562Poč.str. 12 s. Forma vydání Online - E Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova mast-cell tryptase ; Ixodes scapularis ; sialostatin-L Vědní obor RIV EB - Genetika a molekulární biologie CEP GPP302/11/P798 GA ČR - Grantová agentura ČR LH12002 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GAP502/12/2409 GA ČR - Grantová agentura ČR EE2.3.30.0032 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora BC-A - RVO:60077344 UT WOS 000321202100017 DOI 10.1371/journal.pone.0062562 Anotace Background: A salivary proteome-transcriptome project on the hard tick Ixodes scapularis revealed that Kunitz peptides are the most abundant salivary proteins. Ticks use Kunitz peptides (among other salivary proteins) to combat host defense mechanisms and to obtain a blood meal. Most of these Kunitz peptides, however, remain functionally uncharacterized, thus limiting our knowledge about their biochemical interactions. Results: We discovered an unusual cysteine motif in a Kunitz peptide. This peptide inhibits several serine proteases with high affinity and was named tryptogalinin due to its high affinity for beta-tryptase. Compared with other functionally described peptides from the Acari subclass, we showed that tryptogalinin is phylogenetically related to a Kunitz peptide from Rhipicephalus appendiculatus, also reported to have a high affinity for b-tryptase. Using homology-based modeling (and other protein prediction programs) we were able to model and explain the multifaceted function of tryptogalinin. The N-terminus of the modeled tryptogalinin is detached from the rest of the peptide and exhibits intrinsic disorder allowing an increased flexibility for its high affinity with its inhibiting partners (i.e., serine proteases). Conclusions: By incorporating experimental and computational methods our data not only describes the function of a Kunitz peptide from Ixodes scapularis, but also allows us to hypothesize about the molecular basis of this function at the atomic level. Pracoviště Biologické centrum (od r. 2006) Kontakt Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Rok sběru 2014
Počet záznamů: 1