Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

is the causal pathogen of the devastating tomato gray leaf spot with a wide range of alternative plant hosts. To mitigate its potential endemic in facility-cultivated tomatoes, novel disease control strategies should be attempted to minimize the use of chemical fungicides. In this study, we identified a metalloprotease from genome and designated it as SlMEP1, as it appears to be a typical zinc metalloproteinase containing a WLM (WSS1-like metalloprotease) domain and a characteristic HEXXH motif, which we determined by analyzing its transcriptional profile and enzymatic functions. The transcription level of increased greatly during the fungal invasion of tomato leaves. The deletion of the gene from hindered its mycelial growth and reduced its pathogenicity. An assessment of the functional dissection indicated that SlMEP1 induced cell collapse and inhibited the expression of the host chitinases, which consequently made tomato cells more susceptible to and other pathogenic fungi.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC12112490PMC
http://dx.doi.org/10.3390/jof11050330DOI Listing

Publication Analysis

Top Keywords

zinc metalloprotease
4
metalloprotease slmep1
4
slmep1 essential
4
essential factor
4
factor required
4
required fungal
4
fungal virulence
4
virulence causal
4
causal pathogen
4
pathogen devastating
4

Similar Publications

Leishmaniasis is a vector-borne parasitic disease caused by Leishmania spp., for which there is no vaccine and an urgent need for better drugs. The zinc metalloprotease gp63 of Leishmania has been identified as an antigenic structure for vaccine design and a promising target for new antileishmanial agents.

View Article and Find Full Text PDF

Recent studies reveal that Vibrio cholerae secretes virulence factors impacting host cell viability, though their effects on cancer cells remain unclear. However, the bacterial components and mechanisms influencing cancer cells remain largely unknown. This study investigated the effects of V.

View Article and Find Full Text PDF

The zinc containing matrix metalloproteinase enzyme regulates a diverse array of biological processes in health and disease, including ADAM17 (a disintegrin and metalloproteinase domain 17) enzyme. Due to its large substrate profile, ADAM17 is known to regulate diverse pathways of inflammation and adaptive immunity. However, the role of ADAM17 in modulating the pathogenesis of type 2 allergic asthma is largely unknown.

View Article and Find Full Text PDF

Molecular characterization of zinc metalloproteinase Nas-14 from Trichinella spiralis and its participation in intestinal invasion.

PLoS Negl Trop Dis

August 2025

State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University, Changchun, China.

Astacins, a family of zinc metalloproteinases, are involved in invasion and tissue migration processes in a variety of parasites. An astacin-like proteinases have been detected in the excretory-secretory products (ESPs) of Trichinella spiralis (T. spiralis), zinc metalloproteinase Nas-14 (TsNas14), but its function in T.

View Article and Find Full Text PDF

Angiotensin I-converting enzyme (ACE) is a dipeptidyl carboxypeptidase with two homologous catalytic domains [N- and C-domains (nACE and cACE)] that can cleave a range of substrates. cACE primarily cleaves the inactive decapeptide angiotensin I into the potent vasopressor angiotensin II, whereas nACE preferentially cleaves the antifibrotic tetrapeptide N-acetyl-seryl-aspartyl-lysyl-proline (Ac-SDKP). Several ACE inhibitors, which bind to both cACE and nACE active sites, are used clinically for the treatment of hypertension; however, serious side effects are seen in ~ 20-25% of patients due to nonselective inhibition.

View Article and Find Full Text PDF