scholarly journals Functional and structural dissection of the tape measure protein of lactococcal phage TP901-1

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Jennifer Mahony ◽  
Mona Alqarni ◽  
Stephen Stockdale ◽  
Silvia Spinelli ◽  
Marine Feyereisen ◽  
...  
Keyword(s):  
Tape Measure Protein ◽  
Tape Measure

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 Genome Sequences of Gordonia Phages Hotorobo, Woes, and Monty

2016 ◽  
Vol 4 (4) ◽  
Author(s):  
Welkin H. Pope ◽  
Jameson P. Davis ◽  
Sirinya O’Shea ◽  
Anastasia C. Pfeiffer ◽  
Alexandra N. Rich ◽  
...  
Keyword(s):  
Genome Sequences ◽  
Tape Measure Protein ◽  
Tape Measure ◽  
Long Tails

Hotorobo, Woes, and Monty are newly isolated bacteriophages of Gordonia terrae 3612. The three phages are related, and their genomes are similarly sized (76,972 bp, 73,752 bp, and 75,680 bp for Hotorobo, Woes, and Monty, respectively) and organized. They have extremely long tails and among the longest tape measure protein genes described to date.

scholarly journals Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone

2008 ◽  
Vol 191 (3) ◽  
pp. 728-734 ◽  
Author(s):  
Marina Siponen ◽  
Giuliano Sciara ◽  
Manuela Villion ◽  
Silvia Spinelli ◽  
Julie Lichière ◽  
...  
Keyword(s):  
Crystal Packing ◽  
Nonstructural Protein ◽  
Lytic Cycle ◽  
Tape Measure Protein ◽  
Aromatic Residues ◽  
Tape Measure ◽  
Tail Assembly ◽  
Virion Structure ◽  
Repeated Motif

ABSTRACT We report here the characterization of the nonstructural protein ORF12 of the virulent lactococcal phage p2, which belongs to the Siphoviridae family. ORF12 was produced as a soluble protein, which forms large oligomers (6- to 15-mers) in solution. Using anti-ORF12 antibodies, we have confirmed that ORF12 is not found in the virion structure but is detected in the second half of the lytic cycle, indicating that it is a late-expressed protein. The structure of ORF12, solved by single anomalous diffraction and refined at 2.9-Å resolution, revealed a previously unknown fold as well as the presence of a hydrophobic patch at its surface. Furthermore, crystal packing of ORF12 formed long spirals in which a hydrophobic, continuous crevice was identified. This crevice exhibited a repeated motif of aromatic residues, which coincided with the same repeated motif usually found in tape measure protein (TMP), predicted to form helices. A model of a complex between ORF12 and a repeated motif of the TMP of phage p2 (ORF14) was generated, in which the TMP helix fitted exquisitely in the crevice and the aromatic patches of ORF12. We suggest, therefore, that ORF12 might act as a chaperone for TMP hydrophobic repeats, maintaining TMP in solution during the tail assembly of the lactococcal siphophage p2.

scholarly journals The Tape Measure Protein of the Staphylococcus aureus Bacteriophage vB_SauS-phiIPLA35 Has an Active Muramidase Domain

2012 ◽  
Vol 78 (17) ◽  
pp. 6369-6371 ◽  
Author(s):  
Lorena Rodríguez-Rubio ◽  
Dolores Gutiérrez ◽  
Beatriz Martínez ◽  
Ana Rodríguez ◽  
Friedrich Götz ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Lytic Activity ◽  
Structural Proteins ◽  
Tape Measure Protein ◽  
Content Type ◽  
Double Stranded Dna ◽  
Tape Measure ◽  
Hydrolytic Activities ◽  
Muramidase Activity

ABSTRACTTailed double-stranded DNA (dsDNA) bacteriophages frequently harbor structural proteins displaying peptidoglycan hydrolytic activities. The tape measure protein fromStaphylococcus aureusbacteriophage vB_SauS-phiIPLA35 has a lysozyme-like and a peptidase_M23 domain. This report shows that the lysozyme-like domain (TG1) has muramidase activity and exhibitsin vitrolytic activity against liveS. aureuscells, an activity that could eventually find use in the treatment of infections.

scholarly journals X-ray structure of a superinfection exclusion lipoprotein from phage TP-J34 and identification of the tape measure protein as its target

2013 ◽  
Vol 89 (1) ◽  
pp. 152-165 ◽  
Author(s):  
Cecilia Bebeacua ◽  
Juan Carlos Lorenzo Fajardo ◽  
Stéphanie Blangy ◽  
Silvia Spinelli ◽  
Stefanie Bollmann ◽  
...  
Keyword(s):  
Tape Measure Protein ◽  
X Ray ◽  
Superinfection Exclusion ◽  
Tape Measure

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.

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