scholarly journals Conserved and Diverse Traits of Adhesion Devices from Siphoviridae Recognizing Proteinaceous or Saccharidic Receptors

Viruses ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 512 ◽  
Author(s):  
Adeline Goulet ◽  
Silvia Spinelli ◽  
Jennifer Mahony ◽  
Christian Cambillau
Keyword(s):  
Receptor Binding ◽  
Binding Proteins ◽  
Phage Therapy ◽  
Activation Mechanism ◽  
Host Recognition ◽  
Tape Measure Protein ◽  
Tape Measure ◽  
Receptor Recognition ◽  
Contractile Tail ◽  
Tail Protein

Bacteriophages can play beneficial roles in phage therapy and destruction of food pathogens. Conversely, they play negative roles as they infect bacteria involved in fermentation, resulting in serious industrial losses. Siphoviridae phages possess a long non-contractile tail and use a mechanism of infection whose first step is host recognition and binding. They have evolved adhesion devices at their tails’ distal end, tuned to recognize specific proteinaceous or saccharidic receptors on the host’s surface that span a large spectrum of shapes. In this review, we aimed to identify common patterns beyond this apparent diversity. To this end, we analyzed siphophage tail tips or baseplates, evaluating their known structures, where available, and uncovering patterns with bioinformatics tools when they were not. It was thereby identified that a triad formed by three proteins in complex, i.e., the tape measure protein (TMP), the distal tail protein (Dit), and the tail-associated lysozyme (Tal), is conserved in all phages. This common scaffold may harbor various functional extensions internally while it also serves as a platform for plug-in ancillary or receptor-binding proteins (RBPs). Finally, a group of siphophage baseplates involved in saccharidic receptor recognition exhibits an activation mechanism reminiscent of that observed in Myoviridae.

scholarly journals Alteromonas Myovirus V22 Represents a New Genus of Marine Bacteriophages Requiring a Tail Fiber Chaperone for Host Recognition

mSystems ◽  
2020 ◽  
Vol 5 (3) ◽  
Author(s):  
Rafael Gonzalez-Serrano ◽  
Matthew Dunne ◽  
Riccardo Rosselli ◽  
Ana-Belen Martin-Cuadrado ◽  
Virginie Grosboillot ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Receptor Binding ◽  
Binding Proteins ◽  
Fluorescent Protein ◽  
Sequence Similarity ◽  
Functional Characterization ◽  
Size Exclusion ◽  
Host Recognition ◽  
Tail Fiber ◽  
Microbial Composition

ABSTRACT Marine phages play a variety of critical roles in regulating the microbial composition of our oceans. Despite constituting the majority of genetic diversity within these environments, there are relatively few isolates with complete genome sequences or in-depth analyses of their host interaction mechanisms, such as characterization of their receptor binding proteins (RBPs). Here, we present the 92,760-bp genome of the Alteromonas-targeting phage V22. Genomic and morphological analyses identify V22 as a myovirus; however, due to a lack of sequence similarity to any other known myoviruses, we propose that V22 be classified as the type phage of a new Myoalterovirus genus within the Myoviridae family. V22 shows gene homology and synteny with two different subfamilies of phages infecting enterobacteria, specifically within the structural region of its genome. To improve our understanding of the V22 adsorption process, we identified putative RBPs (gp23, gp24, and gp26) and tested their ability to decorate the V22 propagation strain, Alteromonas mediterranea PT11, as recombinant green fluorescent protein (GFP)-tagged constructs. Only GFP-gp26 was capable of bacterial recognition and identified as the V22 RBP. Interestingly, production of functional GFP-gp26 required coexpression with the downstream protein gp27. GFP-gp26 could be expressed alone but was incapable of host recognition. By combining size-exclusion chromatography with fluorescence microscopy, we reveal how gp27 is not a component of the final RBP complex but instead is identified as a new type of phage-encoded intermolecular chaperone that is essential for maturation of the gp26 RBP. IMPORTANCE Host recognition by phage-encoded receptor binding proteins (RBPs) constitutes the first step in all phage infections and the most critical determinant of host specificity. By characterizing new types of RBPs and identifying their essential chaperones, we hope to expand the repertoire of known phage-host recognition machineries. Due to their genetic plasticity, studying RBPs and their associated chaperones can shed new light onto viral evolution affecting phage-host interactions, which is essential for fields such as phage therapy or biotechnology. In addition, since marine phages constitute one of the most important reservoirs of noncharacterized genetic diversity on the planet, their genomic and functional characterization may be of paramount importance for the discovery of novel genes with potential applications.

scholarly journals The Presence of Two Receptor-Binding Proteins Contributes to the Wide Host Range of Staphylococcal Twort-Like Phages

2016 ◽  
Vol 82 (19) ◽  
pp. 5763-5774 ◽  
Author(s):  
Ippei Takeuchi ◽  
Keita Osada ◽  
Aa Haeruman Azam ◽  
Hiroaki Asakawa ◽  
Kazuhiko Miyanaga ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Host Range ◽  
Receptor Binding ◽  
Polyclonal Antibody ◽  
Binding Proteins ◽  
Host Recognition ◽  
Resistant Bacteria ◽  
Tail Fiber ◽  
Content Type ◽  
Wide Host Range

ABSTRACTThanks to their wide host range and virulence, staphylococcal bacteriophages (phages) belonging to the genusTwortlikevirus(staphylococcal Twort-like phages) are regarded as ideal candidates for clinical application forStaphylococcus aureusinfections due to the emergence of antibiotic-resistant bacteria of this species. To increase the usability of these phages, it is necessary to understand the mechanism underlying host recognition, especially the receptor-binding proteins (RBPs) that determine host range. In this study, we found that the staphylococcal Twort-like phage ΦSA012 possesses at least two RBPs. Genomic analysis of five mutant phages of ΦSA012 revealed point mutations inorf103, in a region unique to staphylococcal Twort-like phages. Phages harboring mutated ORF103 could not infectS. aureusstrains in which wall teichoic acids (WTAs) are glycosylated with α-N-acetylglucosamine (α-GlcNAc). A polyclonal antibody against ORF103 also inhibited infection by ΦSA012 in the presence of α-GlcNAc, suggesting that ORF103 binds to α-GlcNAc. In contrast, a polyclonal antibody against ORF105, a short tail fiber component previously shown to be an RBP, inhibited phage infection irrespective of the presence of α-GlcNAc. Immunoelectron microscopy indicated that ORF103 is a tail fiber component localized at the bottom of the baseplate. From these results, we conclude that ORF103 binds α-GlcNAc in WTAs, whereas ORF105, the primary RBP, is likely to bind the WTA backbone. These findings provide insight into the infection mechanism of staphylococcal Twort-like phages.IMPORTANCEStaphylococcusphages belonging to the genusTwortlikevirus(called staphylococcal Twort-like phages) are considered promising agents for control ofStaphylococcus aureusdue to their wide host range and highly lytic capabilities. Although staphylococcal Twort-like phages have been studied widely for therapeutic purposes, the host recognition process of staphylococcal Twort-like phages remains unclear. This work provides new findings about the mechanisms of host recognition of the staphylococcal Twort-like phage ΦSA012. The details of the host recognition mechanism of ΦSA012 will allow us to analyze the mechanisms of infection and expand the utility of staphylococcal Twort-like phages for the control ofS. aureus.

scholarly journals Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen

2017 ◽  
Vol 114 (35) ◽  
pp. E7348-E7357 ◽  
Author(s):  
Jesper Pallesen ◽  
Nianshuang Wang ◽  
Kizzmekia S. Corbett ◽  
Daniel Wrapp ◽  
Robert N. Kirchdoerfer ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Case Fatality ◽  
Neutralizing Antibody ◽  
Human Populations ◽  
Receptor Binding Domain ◽  
Potential Mechanism ◽  
Primary Target ◽  
Humoral Immune ◽  
Receptor Recognition ◽  
Antibody Titers

Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. As in other coronaviruses, the spike (S) glycoprotein of MERS-CoV mediates receptor recognition and membrane fusion and is the primary target of the humoral immune response during infection. Here we use structure-based design to develop a generalizable strategy for retaining coronavirus S proteins in the antigenically optimal prefusion conformation and demonstrate that our engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV. We also determined high-resolution structures of the trimeric MERS-CoV S ectodomain in complex with G4, a stem-directed neutralizing antibody. The structures reveal that G4 recognizes a glycosylated loop that is variable among coronaviruses and they define four conformational states of the trimer wherein each receptor-binding domain is either tightly packed at the membrane-distal apex or rotated into a receptor-accessible conformation. Our studies suggest a potential mechanism for fusion initiation through sequential receptor-binding events and provide a foundation for the structure-based design of coronavirus vaccines.

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

scholarly journals The evolution of the tape measure protein: units, duplications and losses

2011 ◽  
Vol 12 (Suppl 9) ◽  
pp. S10 ◽  
Author(s):  
Mahdi Belcaid ◽  
Anne Bergeron ◽  
Guylaine Poisson
Keyword(s):  
Tape Measure Protein ◽  
Tape Measure

scholarly journals Exploiting phage receptor binding proteins to enable endolysins to kill Gram-negative bacteria

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Athina Zampara ◽  
Martine C. Holst Sørensen ◽  
Dennis Grimon ◽  
Fabio Antenucci ◽  
Amira Ruslanovna Vitt ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Proteins ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Phage Receptor

scholarly journals Carcinoembryonic Antigen Family Receptor Recognition by Gonococcal Opa Proteins Requires Distinct Combinations of Hypervariable Opa Protein Domains

2002 ◽  
Vol 70 (4) ◽  
pp. 1715-1723 ◽  
Author(s):  
Martine P. Bos ◽  
David Kao ◽  
Daniel M. Hogan ◽  
Christopher C. R. Grant ◽  
Robert J. Belland
Keyword(s):  
Carcinoembryonic Antigen ◽  
Receptor Binding ◽  
Binding Activity ◽  
Host Cells ◽  
Sulfate Proteoglycan ◽  
Binding Properties ◽  
Receptor Binding Activity ◽  
Receptor Recognition ◽  
Strain Ms11 ◽  
Gonococcal Strain

ABSTRACT Neisserial Opa proteins function as a family of adhesins that bind heparan sulfate proteoglycan (HSPG) or carcinoembryonic antigen family (CEACAM) receptors on human host cells. In order to define the CEACAM binding domain on Opa proteins, we tested the binding properties of a series of gonococcal (strain MS11) recombinants producing mutant and chimeric Opa proteins with alterations in one or more of the four surface-exposed loops. Mutagenesis demonstrated that the semivariable domain, present in the first loop, was completely dispensable for CEACAM binding. In contrast, the two hypervariable (HV) regions present in the second and third loops were essential for binding; deletion of either domain resulted in loss of receptor recognition. Deletion of the fourth loop resulted in a severe decrease in Opa expression at the cell surface and could therefore not be tested for CEACAM binding. Chimeric Opa variants, containing combinations of HV regions derived from different CEACAM binding Opa proteins, lost most of their receptor binding activity. Some chimeric variants gained HSPG binding activity. Together, our results indicate that full recognition of CEACAM receptors by Opa proteins requires a highly coordinate interplay between both HV regions. Furthermore, shuffling of HV regions may result in novel HSPG receptor binding activity.

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