Potyviral Helper-Component Protease: Multifaced Functions and Interactions with Host Proteins
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00586701" target="_blank" >RIV/61388971:_____/24:00586701 - isvavai.cz</a>
Alternative codes found
RIV/61389030:_____/24:00586701 RIV/00216208:11310/24:10493878
Result on the web
<a href="https://www.mdpi.com/2223-7747/13/9/1236" target="_blank" >https://www.mdpi.com/2223-7747/13/9/1236</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/plants13091236" target="_blank" >10.3390/plants13091236</a>
Alternative languages
Result language
angličtina
Original language name
Potyviral Helper-Component Protease: Multifaced Functions and Interactions with Host Proteins
Original language description
The best-characterized functional motifs of the potyviral Helper-Component protease (HC-Pro) responding for aphid transmission, RNA silencing suppression, movement, symptom development, and replication are gathered in this review. The potential cellular protein targets of plant virus proteases remain largely unknown despite their multifunctionality. The HC-Pro catalytic domain, as a cysteine protease, autoproteolytically cleaves the potyviral polyproteins in the sequence motif YXVG/G and is not expected to act on host targets, however, 146 plant proteins in the Viridiplantae clade containing this motif were searched in the UniProtKB database and are discussed. On the other hand, more than 20 interactions within the entire HC-Pro structure are known. Most of these interactions with host targets (such as the 20S proteasome, methyltransferase, transcription factor eIF4E, and microtubule-associated protein HIP2) modulate the cellular environments for the benefit of virus accumulation or contribute to symptom severity (interactions with MinD, Rubisco, ferredoxin) or participate in the suppression of RNA silencing (host protein VARICOSE, calmodulin-like protein). On the contrary, the interaction of HC-Pro with triacylglycerol lipase, calreticulin, and violaxanthin deepoxidase seems to be beneficial for the host plant. The strength of these interactions between HC-Pro and the corresponding host protein vary with the plant species. Therefore, these interactions may explain the species-specific sensitivity to potyviruses.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
<a href="/en/project/TM04000026" target="_blank" >TM04000026: Effective diagnostic methods for tobamoviruses and tospoviruses, improving disease surveillance and tomato resistance to these pathogens</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Plants
ISSN
2223-7747
e-ISSN
2223-7747
Volume of the periodical
13
Issue of the periodical within the volume
9
Country of publishing house
CH - SWITZERLAND
Number of pages
21
Pages from-to
1236
UT code for WoS article
001219987500001
EID of the result in the Scopus database
2-s2.0-85192785312