Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family

Jēkabs Fridmanis; Mārtiņš Otikovs; Kalvis Brangulis; Kaspars Tārs; Kristaps Jaudzems

doi:10.1002/prot.26011

Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family

Jēkabs Fridmanis, Mārtiņš Otikovs, Kalvis Brangulis, Kaspars Tārs, Kristaps Jaudzems (Corresponding Author)

Department of Human Physiology and Biochemistry

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

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. 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.

Original language	English
Pages (from-to)	588-594
Number of pages	7
Journal	Proteins: Structure, Function and Bioinformatics
Volume	89
Issue number	5
DOIs	https://doi.org/10.1002/prot.26011
Publication status	Published - 1 May 2021

Keywords*

BBP28
cp32 plasmid
mlp family
solution NMR structure
ϕBB-1 phage

Field of Science*

1.6 Biological sciences
3.1 Basic medicine

Publication Type*

1.1. Scientific article indexed in Web of Science and/or Scopus database

Access to Document

10.1002/prot.26011

Cite this

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title = "Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family",

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. 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.",

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author = "Jēkabs Fridmanis and Mārtiņ{\v s} Otikovs and Kalvis Brangulis and Kaspars Tārs and Kristaps Jaudzems",

year = "2021",

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doi = "10.1002/prot.26011",

language = "English",

volume = "89",

pages = "588--594",

journal = "Proteins: Structure, Function and Bioinformatics",

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TY - JOUR

T1 - Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family

AU - Fridmanis, Jēkabs

AU - Otikovs, Mārtiņš

AU - Brangulis, Kalvis

AU - Tārs, Kaspars

AU - Jaudzems, Kristaps

PY - 2021/5/1

Y1 - 2021/5/1

N2 - 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.

AB - 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.

KW - BBP28

KW - cp32 plasmid

KW - mlp family

KW - solution NMR structure

KW - ϕBB-1 phage

UR - http://www.scopus.com/inward/record.url?scp=85091683332&partnerID=8YFLogxK

U2 - 10.1002/prot.26011

DO - 10.1002/prot.26011

M3 - Article

C2 - 32949018

AN - SCOPUS:85091683332

SN - 0887-3585

VL - 89

SP - 588

EP - 594

JO - Proteins: Structure, Function and Bioinformatics

JF - Proteins: Structure, Function and Bioinformatics

IS - 5

ER -

Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family

Abstract

Keywords*

Field of Science*

Publication Type*

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