scholarly journals Mapping the Tail Fiber as the Receptor Binding Protein Responsible for Differential Host Specificity of Pseudomonas aeruginosa Bacteriophages PaP1 and JG004

PLoS ONE ◽  
2013 ◽  
Vol 8 (7) ◽  
pp. e68562 ◽  
Author(s):  
Shuai Le ◽  
Xuesong He ◽  
Yinling Tan ◽  
Guangtao Huang ◽  
Lin Zhang ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Host Specificity ◽  
Receptor Binding ◽  
Binding Protein ◽  
Tail Fiber ◽  
Differential Host ◽  
Receptor Binding Protein

scholarly journals A Tail Fiber Protein and a Receptor-Binding Protein Mediate ICP2 Bacteriophage Interactions with Vibrio cholerae OmpU

2021 ◽  
Author(s):  
Andrea N.W. Lim ◽  
Minmin Yen ◽  
Kimberley D. Seed ◽  
David W. Lazinski ◽  
Andrew Camilli
Keyword(s):  
Host Range ◽  
Vibrio Cholerae ◽  
Receptor Binding ◽  
Binding Protein ◽  
Mutant Phenotype ◽  
Tail Fiber ◽  
Missense Mutations ◽  
Wild Type ◽  
Stool Samples ◽  
Receptor Binding Protein

AbstractICP2 is a virulent bacteriophage (phage) that preys on Vibrio cholerae. ICP2 was first isolated from cholera patient stool samples. Some of these stools also contained ICP2-resistant isogenic V. cholerae strains harboring missense mutations in the trimeric outer membrane porin protein OmpU, identifying it as the ICP2 receptor. In this study, we identify the ICP2 proteins that mediate interactions with OmpU by selecting for ICP2 host-range mutants within infant rabbits infected with a mixture of wild type and OmpU mutant strains. ICP2 host-range mutants had missense mutations in putative tail fiber gene gp25 and putative adhesin gp23. Using site-specific mutagenesis we show that single or double mutations in gp25 are sufficient to generate the host-range mutant phenotype. However, at least one additional mutation in gp23 is required for robust plaque formation on specific OmpU mutants. Mutations in gp23 alone were insufficient to give a host-range mutant phenotype. All ICP2 host-range mutants retained the ability to plaque on wild type V. cholerae cells. The strength of binding of host-range mutants to V. cholerae correlated with plaque morphology, indicating that the selected mutations in gp25 and gp23 restore molecular interactions with the receptor. We propose that ICP2 host-range mutants evolve by a two-step process where, first, gp25 mutations are selected for their broad host-range, albeit accompanied by low level phage adsorption. Subsequent selection occurs for gp23 mutations that further increase productive binding to specific OmpU alleles, allowing for near wild type efficiencies of adsorption and subsequent phage multiplication.ImportanceConcern over multidrug-resistant bacterial pathogens, including Vibrio cholerae, has led to a renewed interest in phage biology and their potential for phage therapy. ICP2 is a genetically unique virulent phage isolated from cholera patient stool samples. It is also one of three phages in a prophylactic cocktail shown to be effective in animal models of infection and the only one of the three that requires a protein receptor (OmpU). This study identifies a ICP2 tail fiber and a receptor binding protein and examines how ICP2 responds to the selective pressures of phage-resistant OmpU mutants. We found that this particular co-evolutionary arms race presents fitness costs to both ICP2 and V. cholerae.

scholarly journals F1Aα, a Death Receptor-binding Protein Homologous to theCaenorhabditis elegansSex-determining Protein, FEM-1, Is a Caspase Substrate That Mediates Apoptosis

1999 ◽  
Vol 274 (45) ◽  
pp. 32461-32468 ◽  
Author(s):  
Shing-Leng Chan ◽  
Kuan-Onn Tan ◽  
Li Zhang ◽  
Karen S. Y. Yee ◽  
Francesca Ronca ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Protein ◽  
Death Receptor ◽  
Caspase Substrate ◽  
Receptor Binding Protein

Specific detection of Campylobacter jejuni using the bacteriophage NCTC 12673 receptor binding protein as a probe

The Analyst ◽  
2011 ◽  
Vol 136 (22) ◽  
pp. 4780 ◽  
Author(s):  
Amit Singh ◽  
Denis Arutyunov ◽  
Mark T. McDermott ◽  
Christine M. Szymanski ◽  
Stephane Evoy
Keyword(s):  
Campylobacter Jejuni ◽  
Receptor Binding ◽  
Binding Protein ◽  
Specific Detection ◽  
Receptor Binding Protein

Receptor binding protein amperometric affinity sensor for rapid β-lactam quantification in milk

1999 ◽  
Vol 398 (1) ◽  
pp. 13-22 ◽  
Author(s):  
S.J. Setford ◽  
R.M. Van Es ◽  
Y.J. Blankwater ◽  
S. Kröger
Keyword(s):  
Receptor Binding ◽  
Binding Protein ◽  
Receptor Binding Protein

scholarly journals A receptor-binding protein ofCampylobacter jejunibacteriophage NCTC 12673 recognizes flagellin glycosylated with acetamidino-modified pseudaminic acid

2014 ◽  
Vol 95 (1) ◽  
pp. 101-115 ◽  
Author(s):  
Muhammad Afzal Javed ◽  
Lieke B. van Alphen ◽  
Jessica Sacher ◽  
Wen Ding ◽  
John Kelly ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Protein ◽  
Pseudaminic Acid ◽  
Receptor Binding Protein

scholarly journals Peroxisome-proliferator-activated receptor-binding protein (PBP) is essential for the growth of active Notch4-immortalized mammary epithelial cells by activating SOX10 expression

2009 ◽  
Vol 425 (2) ◽  
pp. 435-444 ◽  
Author(s):  
Yiwei Tony Zhu ◽  
Yuzhi Jia ◽  
Liping Hu ◽  
Chao Qi ◽  
Megana K. Prasad ◽  
...  
Keyword(s):  
Growth Inhibition ◽  
Receptor Binding ◽  
Binding Protein ◽  
Active Form ◽  
Mammary Epithelial ◽  
Peroxisome Proliferator ◽  
Mammary Cells ◽  
Peroxisome Proliferator Activated Receptor ◽  
Sox10 Expression ◽  
Receptor Binding Protein

PBP (peroxisome-proliferator-activated receptor-binding protein) [Med1 (mediator 1)/TRAP220 (thyroid-hormone-receptor-associated protein 220)] is essential for mammary gland development. We established a mammary epithelial cell line with a genotype of PBPLoxP/LoxP by expressing an active form of Notch4. Null mutation of PBP caused severe growth inhibition of the Notch4-immortalized mammary cells. We found that truncated PBP without the two LXXLL motifs could reverse the growth inhibition due to the deficiency of endogenous PBP, indicating that signalling through nuclear receptors is unlikely to be responsible for the growth inhibition as the result of PBP deficiency. Loss of PBP expression was shown to completely ablate the expression of SOX10 [Sry-related HMG (high-mobility group) box gene 10]. The re-expression of SOX10 was capable of reversing the growth inhibition due to PBP deficiency, whereas suppressed expression of SOX10 inhibited the growth of Notch4-immortalized mammary cells. Further studies revealed PBP is directly recruited to the enhancer of the SOX10 gene, indicating that SOX10 is a direct target gene of PBP. We conclude that PBP is essential for the growth of Notch4-immortalized mammary cells by activating SOX10 expression, providing a potential molecular mechanism through which PBP regulates the growth of mammary stem/progenitor cells.

scholarly journals Regulation of synaptic structure and function by palmitoylated AMPA receptor binding protein

2010 ◽  
Vol 43 (4) ◽  
pp. 341-352 ◽  
Author(s):  
Charu Misra ◽  
Sophie Restituito ◽  
Jainne Ferreira ◽  
Gerald A. Rameau ◽  
Jie Fu ◽  
...  
Keyword(s):  
Ampa Receptor ◽  
Receptor Binding ◽  
Binding Protein ◽  
Structure And Function ◽  
Synaptic Structure ◽  
Ampa Receptor Binding Protein ◽  
And Function ◽  
Receptor Binding Protein
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