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

scholarly journals Developing Innolysins Against Campylobacter jejuni Using a Novel Prophage Receptor-Binding Protein

2021 ◽  
Vol 12 ◽  
Author(s):  
Athina Zampara ◽  
Martine C. Holst Sørensen ◽  
Yilmaz Emre Gencay ◽  
Dennis Grimon ◽  
Sebastian Hougaard Kristiansen ◽  
...  
Keyword(s):  
Campylobacter Jejuni ◽  
Receptor Binding ◽  
Capsular Polysaccharide ◽  
Binding Protein ◽  
Log Reduction ◽  
Cell Counts ◽  
Phage Receptor ◽  
Receptor Binding Protein

Campylobacter contaminated poultry remains the major cause of foodborne gastroenteritis worldwide, calling for novel antibacterials. We previously developed the concept of Innolysin composed of an endolysin fused to a phage receptor binding protein (RBP) and provided the proof-of-concept that Innolysins exert bactericidal activity against Escherichia coli. Here, we have expanded the Innolysin concept to target Campylobacter jejuni. As no C. jejuni phage RBP had been identified so far, we first showed that the H-fiber originating from a CJIE1-like prophage of C. jejuni CAMSA2147 functions as a novel RBP. By fusing this H-fiber to phage T5 endolysin, we constructed Innolysins targeting C. jejuni (Innolysins Cj). Innolysin Cj1 exerts antibacterial activity against diverse C. jejuni strains after in vitro exposure for 45 min at 20°C, reaching up to 1.30 ± 0.21 log reduction in CAMSA2147 cell counts. Screening of a library of Innolysins Cj composed of distinct endolysins for growth inhibition, allowed us to select Innolysin Cj5 as an additional promising antibacterial candidate. Application of either Innolysin Cj1 or Innolysin Cj5 on chicken skin refrigerated to 5°C and contaminated with C. jejuni CAMSA2147 led to 1.63 ± 0.46 and 1.18 ± 0.10 log reduction of cells, respectively, confirming that Innolysins Cj can kill C. jejuni in situ. The receptor of Innolysins Cj remains to be identified, however, the RBP component (H-fiber) recognizes a novel receptor compared to lytic phages binding to capsular polysaccharide or flagella. Identification of other unexplored Campylobacter phage RBPs may further increase the repertoire of new Innolysins Cj targeting distinct receptors and working as antibacterials against Campylobacter.

scholarly journals Bacteriophage Receptor Binding Protein Based Assays for the Simultaneous Detection of Campylobacter jejuni and Campylobacter coli

PLoS ONE ◽  
2013 ◽  
Vol 8 (7) ◽  
pp. e69770 ◽  
Author(s):  
Muhammad A. Javed ◽  
Somayyeh Poshtiban ◽  
Denis Arutyunov ◽  
Stephane Evoy ◽  
Christine M. Szymanski
Keyword(s):  
Campylobacter Jejuni ◽  
Receptor Binding ◽  
Binding Protein ◽  
Simultaneous Detection ◽  
Campylobacter Coli ◽  
Receptor Binding Protein

scholarly journals Genome and Proteome of Campylobacter jejuni Bacteriophage NCTC 12673

2011 ◽  
Vol 77 (23) ◽  
pp. 8265-8271 ◽  
Author(s):  
Andrew M. Kropinski ◽  
Denis Arutyunov ◽  
Mary Foss ◽  
Anna Cunningham ◽  
Wen Ding ◽  
...  
Keyword(s):  
Campylobacter Jejuni ◽  
Receptor Binding ◽  
Pathogen Detection ◽  
Phage Genome ◽  
Binding Protein ◽  
Pcr Amplification ◽  
Homing Endonucleases ◽  
Bacterial Detection ◽  
Content Type ◽  
Receptor Binding Protein

ABSTRACTCampylobacter jejunicontinues to be the leading cause of bacterial food-borne illness worldwide, so improvements to current methods used for bacterial detection and disease prevention are needed. We describe here the genome and proteome ofC. jejunibacteriophage NCTC 12673 and the exploitation of its receptor-binding protein for specific bacterial detection. Remarkably, the 135-kbMyoviridaegenome of NCTC 12673 differs greatly from any other proteobacterial phage genome described (includingC. jejuniphages CP220 and CPt10) and instead shows closest homology to the cyanobacterial T4-related myophages. The phage genome contains 172 putative open reading frames, including 12 homing endonucleases, no visible means of packaging, and a putativetrans-splicing intein. The phage DNA appears to be strongly associated with a protein that interfered with PCR amplification and estimation of the phage genome mass by pulsed-field gel electrophoresis. Identification and analyses of the receptor-binding protein (Gp48) revealed features common to theSalmonella entericaP22 phage tailspike protein, including the ability to specifically recognize a host organism. Bacteriophage receptor-binding proteins may offer promising alternatives for use in pathogen detection platforms.

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

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.

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