scholarly journals A tail of two phages: genomic and functional analysis of Listeria monocytogenes phages vB_LmoS_188 and vB_LmoS_293 reveal the receptor-binding proteins involved in host specificity

2015 ◽  
Vol 6 ◽  
Author(s):  
Aidan Casey ◽  
Kieran Jordan ◽  
Horst Neve ◽  
Aidan Coffey ◽  
Olivia McAuliffe
Keyword(s):  
Functional Analysis ◽  
Listeria Monocytogenes ◽  
Host Specificity ◽  
Receptor Binding ◽  
Binding Proteins

scholarly journals Glycotyping and Specific Separation of Listeria monocytogenes with a Novel Bacteriophage Protein Tool Kit

2020 ◽  
Vol 86 (13) ◽  
Author(s):  
Eric T. Sumrall ◽  
Christian Röhrig ◽  
Mario Hupfeld ◽  
Lavanja Selvakumar ◽  
Jiemin Du ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Receptor Binding ◽  
Food Industry ◽  
Binding Proteins ◽  
New Technologies ◽  
Teichoic Acid ◽  
Complex Nature ◽  
Glycosylation Pattern ◽  
Content Type ◽  
Novel Method

ABSTRACT The Gram-positive pathogen Listeria monocytogenes can be subdivided into at least 12 different serovars, based on the differential expression of a set of somatic and flagellar antigens. Of note, strains belonging to serovars 1/2a, 1/2b, and 4b cause the vast majority of foodborne listeriosis cases and outbreaks. The standard protocol for serovar determination involves an agglutination method using a set of sera containing cell surface-recognizing antibodies. However, this procedure is imperfect in both precision and practicality, due to discrepancies resulting from subjective interpretation. Furthermore, the exact antigenic epitopes remain unclear, due to the preparation of the absorbed sera and the complex nature of polyvalent antibody binding. Here, we present a novel method for quantitative somatic antigen differentiation using a set of recombinant affinity proteins (cell wall-binding domains and receptor-binding proteins) derived from a collection of Listeria bacteriophages. These proteins enable rapid, objective, and precise identification of the different teichoic acid glycopolymer structures, which represent the O-antigens, and allow a near-complete differentiation. This glycotyping approach confirmed serovar designations of over 60 previously characterized Listeria strains. Using select phage receptor-binding proteins coupled to paramagnetic beads, we also demonstrate the ability to specifically isolate serovar 1/2 or 4b cells from a mixed culture. In addition, glycotyping led to the discovery that strains designated serovar 4e actually possess an intermediate 4b-4d teichoic acid glycosylation pattern, underpinning the high discerning power and precision of this novel technique. IMPORTANCE Listeria monocytogenes is a ubiquitous opportunistic pathogen that presents a major concern to the food industry due to its propensity to cause foodborne illness. The Listeria genus contains 15 different serovars, with most of the variance depending on the wall-associated teichoic acid glycopolymers, which confer somatic antigenicity. Strains belonging to serovars 1/2 and 4b cause the vast majority of listeriosis cases and outbreaks, meaning that regulators, as well as the food industry itself, have an interest in rapidly identifying isolates of these particular serovars in food processing environments. Current methods for phenotypic serovar differentiation are slow and lack accuracy, and the food industry could benefit from new technologies allowing serovar-specific isolation. Therefore, the novel method described here for rapid glycotype determination could present a valuable asset to detect and control this bacterium.

scholarly journals Receptor binding proteins of Listeria monocytogenes bacteriophages A118 and P35 recognize serovar-specific teichoic acids

Virology ◽  
2015 ◽  
Vol 477 ◽  
pp. 110-118 ◽  
Author(s):  
Regula Bielmann ◽  
Matthias Habann ◽  
Marcel R. Eugster ◽  
Rudi Lurz ◽  
Richard Calendar ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Receptor Binding ◽  
Binding Proteins ◽  
Teichoic Acids

scholarly journals Functional analysis of the receptor binding domain of SARS coronavirus S1 region and its monoclonal antibody

2014 ◽  
Vol 36 (3) ◽  
pp. 387-397 ◽  
Author(s):  
Hyun Kim ◽  
Yeongjin Hong ◽  
Keigo Shibayama ◽  
Yasuhiko Suzuki ◽  
Nobutaka Wakamiya ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Functional Analysis ◽  
Receptor Binding ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Sars Coronavirus

scholarly journals A single amino acid in E-cadherin responsible for host specificity towards the human pathogen Listeria monocytogenes

1999 ◽  
Vol 18 (14) ◽  
pp. 3956-3963 ◽  
Author(s):  
Marc Lecuit ◽  
Shaynoor Dramsi ◽  
Cara Gottardi ◽  
Mary Fedor-Chaiken ◽  
Barry Gumbiner ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Amino Acid ◽  
Host Specificity ◽  
Single Amino Acid ◽  
Human Pathogen ◽  
E Cadherin

Functional analysis of membrane vesicles of Listeria monocytogenes suggests a possible role in virulence and physiological stress response

2020 ◽  
Vol 142 ◽  
pp. 104076 ◽  
Author(s):  
Raman Karthikeyan ◽  
Pratapa Gayathri ◽  
Paramasamy Gunasekaran ◽  
Medicharla V. Jagannadham ◽  
Jeyaprakash Rajendhran
Keyword(s):  
Functional Analysis ◽  
Listeria Monocytogenes ◽  
Stress Response ◽  
Physiological Stress ◽  
Membrane Vesicles ◽  
Physiological Stress Response

APPLs: More than just adiponectin receptor binding proteins

2017 ◽  
Vol 32 ◽  
pp. 76-84 ◽  
Author(s):  
Zhuoying Liu ◽  
Ting Xiao ◽  
Xiaoyu Peng ◽  
Guangdi Li ◽  
Fang Hu
Keyword(s):  
Receptor Binding ◽  
Binding Proteins ◽  
Adiponectin Receptor
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