ArticleMicrobiology spectrum2021
Csp1, a Cold Shock Protein Homolog in Xylella fastidiosa Influences Cell Attachment, Pili Formation, and Gene Expression.
Article in Microbiology spectrum, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- From Genome Inspection to Precision Agrochemicals: A Structure-Based Antivirulence Roadmap for Sustainable Crop Protection againstJournal of agricultural and food chemistry · 2026Review
- Cold Shock Proteins Balance Biofilm-Associated Antibiotic Resistance and Oxidative Vulnerability in Mycobacteria.Microorganisms · 2025Article
- Preliminary transcriptomic analyses revealFrontiers in microbiology · 2025Article
- Natural variation of immune epitopes reveals intrabacterial antagonism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- From Stress Tolerance to Virulence: Recognizing the Roles of Csps in Pathogenicity and Food Contamination.Pathogens (Basel, Switzerland) · 2024Review
- A general overview of the multifactorial adaptation to cold: biochemical mechanisms and strategies.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Review
- Comparative Proteomic Analysis of Protein Patterns ofMicroorganisms · 2023Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial cold shock-domain proteins are conserved nucleic acid binding chaperones that play important roles in stress adaptation and pathogenesis. Csp1 is a temperature-independent cold shock protein homolog in Xylella fastidiosa, a bacterial plant pathogen of grapevine and other economically important crops. Csp1 contributes to stress tolerance and virulence in X. fastidiosa. However, besides general single-stranded nucleic acid binding activity, little is known about the specific function(s) of Csp1. To further investigate the role(s) of Csp1, we compared phenotypic differences and transcriptome profiles between the wild type and a
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