4hem: Difference between revisions
New page: '''Unreleased structure''' The entry 4hem is ON HOLD Authors: Desmyter, A., Spinelli, S., Farenc, c., Blangy, S., Bebeacua, C., van Sinderen, D., Mahony, J., Cambillau, C Description: ... |
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==Llama vHH-02 binder of ORF49 (RBP) from lactococcal phage TP901-1== | |||
<StructureSection load='4hem' size='340' side='right'caption='[[4hem]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hem]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_phage_TP901-1 Lactococcus phage TP901-1] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hem OCA], [https://pdbe.org/4hem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hem RCSB], [https://www.ebi.ac.uk/pdbsum/4hem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hem ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9G096_9CAUD Q9G096_9CAUD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lactococcal phages belong to a large family of Siphoviridae and infect Lactococcus lactis, a gram-positive bacterium used in commercial dairy fermentations. These phages are believed to recognize and bind specifically to pellicle polysaccharides covering the entire bacterium. The phage TP901-1 baseplate, located at the tip of the tail, harbors 18 trimeric receptor binding proteins (RBPs) promoting adhesion to a specific lactococcal strain. Phage TP901-1 adhesion does not require major conformational changes or Ca(2+), which contrasts other lactococcal phages. Here, we produced and characterized llama nanobodies raised against the purified baseplate and the Tal protein of phage TP901-1 as tools to dissect the molecular determinants of phage TP901-1 infection. Using a set of complementary techniques, surface plasmon resonance, EM, and X-ray crystallography in a hybrid approach, we identified binders to the three components of the baseplate, analyzed their affinity for their targets, and determined their epitopes as well as their functional impact on TP901-1 phage infectivity. We determined the X-ray structures of three nanobodies in complex with the RBP. Two of them bind to the saccharide binding site of the RBP and are able to fully neutralize TP901-1 phage infectivity, even after 15 passages. These results provide clear evidence for a practical use of nanobodies in circumventing lactococcal phages viral infection in dairy fermentation. | |||
Viral infection modulation and neutralization by camelid nanobodies.,Desmyter A, Farenc C, Mahony J, Spinelli S, Bebeacua C, Blangy S, Veesler D, van Sinderen D, Cambillau C Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):E1371-9. doi:, 10.1073/pnas.1301336110. Epub 2013 Mar 25. PMID:23530214<ref>PMID:23530214</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hem" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[3D structures of non-human antibody|3D structures of non-human antibody]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactococcus phage TP901-1]] | |||
[[Category: Lama glama]] | |||
[[Category: Large Structures]] | |||
[[Category: Bebeacua C]] | |||
[[Category: Blangy S]] | |||
[[Category: Cambillau C]] | |||
[[Category: Desmyter A]] | |||
[[Category: Farenc C]] | |||
[[Category: Mahony J]] | |||
[[Category: Spinelli S]] | |||
[[Category: Van Sinderen D]] | |||
Latest revision as of 17:07, 8 November 2023
Llama vHH-02 binder of ORF49 (RBP) from lactococcal phage TP901-1Llama vHH-02 binder of ORF49 (RBP) from lactococcal phage TP901-1
Structural highlights
FunctionPublication Abstract from PubMedLactococcal phages belong to a large family of Siphoviridae and infect Lactococcus lactis, a gram-positive bacterium used in commercial dairy fermentations. These phages are believed to recognize and bind specifically to pellicle polysaccharides covering the entire bacterium. The phage TP901-1 baseplate, located at the tip of the tail, harbors 18 trimeric receptor binding proteins (RBPs) promoting adhesion to a specific lactococcal strain. Phage TP901-1 adhesion does not require major conformational changes or Ca(2+), which contrasts other lactococcal phages. Here, we produced and characterized llama nanobodies raised against the purified baseplate and the Tal protein of phage TP901-1 as tools to dissect the molecular determinants of phage TP901-1 infection. Using a set of complementary techniques, surface plasmon resonance, EM, and X-ray crystallography in a hybrid approach, we identified binders to the three components of the baseplate, analyzed their affinity for their targets, and determined their epitopes as well as their functional impact on TP901-1 phage infectivity. We determined the X-ray structures of three nanobodies in complex with the RBP. Two of them bind to the saccharide binding site of the RBP and are able to fully neutralize TP901-1 phage infectivity, even after 15 passages. These results provide clear evidence for a practical use of nanobodies in circumventing lactococcal phages viral infection in dairy fermentation. Viral infection modulation and neutralization by camelid nanobodies.,Desmyter A, Farenc C, Mahony J, Spinelli S, Bebeacua C, Blangy S, Veesler D, van Sinderen D, Cambillau C Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):E1371-9. doi:, 10.1073/pnas.1301336110. Epub 2013 Mar 25. PMID:23530214[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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