Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family
Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2021-05, Vol.89 (5), p.588-594 |
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| container_title | Proteins, structure, function, and bioinformatics |
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| creator | Fridmanis, Jēkabs Otikovs, Mārtiņš Brangulis, Kalvis Tārs, Kaspars Jaudzems, Kristaps |
| description | Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five α‐helices and an extended C‐terminal loop. The fold is similar to that of Borrelia turicatae outer surface protein BTA121, which is known to bind lipids. These results contribute to the understanding of Lyme disease pathogenesis by revealing the molecular structure of a protein from the widely found mlp family. |
| doi_str_mv | 10.1002/prot.26011 |
| format | Article |
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We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five α‐helices and an extended C‐terminal loop. The fold is similar to that of Borrelia turicatae outer surface protein BTA121, which is known to bind lipids. 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Otikovs, Mārtiņš ; Brangulis, Kalvis ; Tārs, Kaspars ; Jaudzems, Kristaps</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3571-fd69719cec3a5819860f6955d5ea0cd4c9691deb9282123ae587f2e068315203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>BBP28</topic><topic>Borrelia burgdorferi</topic><topic>cp32 plasmid</topic><topic>Disease transmission</topic><topic>Helices</topic><topic>Lipids</topic><topic>Lipoproteins</topic><topic>Lyme disease</topic><topic>mlp family</topic><topic>Mlp protein</topic><topic>Molecular structure</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Pathogenesis</topic><topic>Protein folding</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>solution NMR structure</topic><topic>Spirochetes</topic><topic>Vector-borne diseases</topic><topic>ϕBB‐1 phage</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fridmanis, Jēkabs</creatorcontrib><creatorcontrib>Otikovs, Mārtiņš</creatorcontrib><creatorcontrib>Brangulis, Kalvis</creatorcontrib><creatorcontrib>Tārs, Kaspars</creatorcontrib><creatorcontrib>Jaudzems, Kristaps</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Proteins, structure, function, and bioinformatics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fridmanis, Jēkabs</au><au>Otikovs, Mārtiņš</au><au>Brangulis, Kalvis</au><au>Tārs, Kaspars</au><au>Jaudzems, Kristaps</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>2021-05</date><risdate>2021</risdate><volume>89</volume><issue>5</issue><spage>588</spage><epage>594</epage><pages>588-594</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><abstract>Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. 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| ispartof | Proteins, structure, function, and bioinformatics, 2021-05, Vol.89 (5), p.588-594 |
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| language | eng |
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| source | Wiley Online Library All Journals |
| subjects | BBP28 Borrelia burgdorferi cp32 plasmid Disease transmission Helices Lipids Lipoproteins Lyme disease mlp family Mlp protein Molecular structure NMR Nuclear magnetic resonance Pathogenesis Protein folding Protein structure Proteins solution NMR structure Spirochetes Vector-borne diseases ϕBB‐1 phage |
| title | Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family |
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