Identification of proteins exhibiting in vitro RNA chaperone activity through gradient profiling in the Lyme disease spirochete, Borrelia burgdorferi

Taylor Van Gundy; Cornelius Schneider; Christopher C. Ebmeier; Gavin Z. Chambers; Nicholas A. Cramer; Kathryn M.F. Chambers; Dan Drecktrah; Jenny A. Hyde; Jon T. Skare; Richard T. Marconi; D. Scott Samuels; Meghan C. Lybecker

doi:10.1080/15476286.2026.2684395

Identification of proteins exhibiting in vitro RNA chaperone activity through gradient profiling in the Lyme disease spirochete, Borrelia burgdorferi

Taylor Van Gundy
, Cornelius Schneider
, Christopher C. Ebmeier
, Gavin Z. Chambers
, Nicholas A. Cramer
, Kathryn M.F. Chambers
, Dan Drecktrah
, Jenny A. Hyde
, Jon T. Skare
, Richard T. Marconi
, D. Scott Samuels
, Meghan C. Lybecker

Division of Biological and Biomedical Sciences

Centers for Disease Control and Prevention
University of Würzburg
University of Colorado Boulder
Virginia Commonwealth University
Texas A&M University

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

Abstract

RNA-binding proteins (RBPs) play key roles in regulating gene expression across all domains of life. However, relatively few RBPs have been discovered and characterized in Borrelia (Borreliella) burgdorferi, the causative agent of Lyme disease. We utilized gradient profiling to identify putative RBPs that co-sediment with small RNAs (sRNAs) and nascent mRNAs. The previously hypothetical proteins BB0749, BB0713 and BB0796, as well as the chemotaxis-related protein CheY2 and the flagella-associated protein FlgV demonstrated RNA unwinding (structural remodeling), RNA annealing, and strand displacement activity. Moreover, in vivo co-IP assays demonstrated BB0749 binds RNA in B. burgdorferi.

Original language	English
Pages (from-to)	1-23
Number of pages	23
Journal	RNA Biology
Volume	23
Issue number	1
DOIs	https://doi.org/10.1080/15476286.2026.2684395
State	Published - Jun 2026

Keywords

Borrelia burgdorferi
co-immunoprecipitation
Lyme disease
RNA chaperone
RNA-binding protein
Borrelia burgdorferi/metabolism
RNA, Bacterial/metabolism
RNA, Messenger/metabolism
RNA-Binding Proteins/metabolism
Bacterial Proteins/metabolism
Lyme Disease/microbiology
Molecular Chaperones/metabolism
Protein Binding
Gene Expression Regulation, Bacterial

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10.1080/15476286.2026.2684395

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Van Gundy, T., Schneider, C., Ebmeier, C. C., Chambers, G. Z., Cramer, N. A., Chambers, K. M. F., Drecktrah, D., Hyde, J. A., Skare, J. T., Marconi, R. T., Samuels, D. S., & Lybecker, M. C. (2026). Identification of proteins exhibiting in vitro RNA chaperone activity through gradient profiling in the Lyme disease spirochete, Borrelia burgdorferi. RNA Biology, 23(1), 1-23. https://doi.org/10.1080/15476286.2026.2684395

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title = "Identification of proteins exhibiting in vitro RNA chaperone activity through gradient profiling in the Lyme disease spirochete, Borrelia burgdorferi",

abstract = "RNA-binding proteins (RBPs) play key roles in regulating gene expression across all domains of life. However, relatively few RBPs have been discovered and characterized in Borrelia (Borreliella) burgdorferi, the causative agent of Lyme disease. We utilized gradient profiling to identify putative RBPs that co-sediment with small RNAs (sRNAs) and nascent mRNAs. The previously hypothetical proteins BB0749, BB0713 and BB0796, as well as the chemotaxis-related protein CheY2 and the flagella-associated protein FlgV demonstrated RNA unwinding (structural remodeling), RNA annealing, and strand displacement activity. Moreover, in vivo co-IP assays demonstrated BB0749 binds RNA in B. burgdorferi.",

keywords = "Borrelia burgdorferi, co-immunoprecipitation, Lyme disease, RNA chaperone, RNA-binding protein, Borrelia burgdorferi/metabolism, RNA, Bacterial/metabolism, RNA, Messenger/metabolism, RNA-Binding Proteins/metabolism, Bacterial Proteins/metabolism, Lyme Disease/microbiology, Molecular Chaperones/metabolism, Protein Binding, Gene Expression Regulation, Bacterial",

author = "\{Van Gundy\}, Taylor and Cornelius Schneider and Ebmeier, \{Christopher C.\} and Chambers, \{Gavin Z.\} and Cramer, \{Nicholas A.\} and Chambers, \{Kathryn M.F.\} and Dan Drecktrah and Hyde, \{Jenny A.\} and Skare, \{Jon T.\} and Marconi, \{Richard T.\} and Samuels, \{D. Scott\} and Lybecker, \{Meghan C.\}",

note = "Publisher Copyright: {\textcopyright} This work was authored as part of the Contributor{\textquoteright}s official duties as an Employee of the United States Government and is therefore a work of the United States Government. In accordance with 17 U.S.C. 105, no copyright protection is available for such works under U.S. Law.",

year = "2026",

month = jun,

doi = "10.1080/15476286.2026.2684395",

language = "English",

volume = "23",

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Van Gundy, T, Schneider, C, Ebmeier, CC, Chambers, GZ, Cramer, NA, Chambers, KMF, Drecktrah, D, Hyde, JA, Skare, JT, Marconi, RT, Samuels, DS & Lybecker, MC 2026, 'Identification of proteins exhibiting in vitro RNA chaperone activity through gradient profiling in the Lyme disease spirochete, Borrelia burgdorferi', RNA Biology, vol. 23, no. 1, pp. 1-23. https://doi.org/10.1080/15476286.2026.2684395

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T1 - Identification of proteins exhibiting in vitro RNA chaperone activity through gradient profiling in the Lyme disease spirochete, Borrelia burgdorferi

AU - Van Gundy, Taylor

AU - Schneider, Cornelius

AU - Ebmeier, Christopher C.

AU - Chambers, Gavin Z.

AU - Cramer, Nicholas A.

AU - Chambers, Kathryn M.F.

AU - Drecktrah, Dan

AU - Hyde, Jenny A.

AU - Skare, Jon T.

AU - Marconi, Richard T.

AU - Samuels, D. Scott

AU - Lybecker, Meghan C.

N1 - Publisher Copyright: © This work was authored as part of the Contributor’s official duties as an Employee of the United States Government and is therefore a work of the United States Government. In accordance with 17 U.S.C. 105, no copyright protection is available for such works under U.S. Law.

PY - 2026/6

Y1 - 2026/6

N2 - RNA-binding proteins (RBPs) play key roles in regulating gene expression across all domains of life. However, relatively few RBPs have been discovered and characterized in Borrelia (Borreliella) burgdorferi, the causative agent of Lyme disease. We utilized gradient profiling to identify putative RBPs that co-sediment with small RNAs (sRNAs) and nascent mRNAs. The previously hypothetical proteins BB0749, BB0713 and BB0796, as well as the chemotaxis-related protein CheY2 and the flagella-associated protein FlgV demonstrated RNA unwinding (structural remodeling), RNA annealing, and strand displacement activity. Moreover, in vivo co-IP assays demonstrated BB0749 binds RNA in B. burgdorferi.

AB - RNA-binding proteins (RBPs) play key roles in regulating gene expression across all domains of life. However, relatively few RBPs have been discovered and characterized in Borrelia (Borreliella) burgdorferi, the causative agent of Lyme disease. We utilized gradient profiling to identify putative RBPs that co-sediment with small RNAs (sRNAs) and nascent mRNAs. The previously hypothetical proteins BB0749, BB0713 and BB0796, as well as the chemotaxis-related protein CheY2 and the flagella-associated protein FlgV demonstrated RNA unwinding (structural remodeling), RNA annealing, and strand displacement activity. Moreover, in vivo co-IP assays demonstrated BB0749 binds RNA in B. burgdorferi.

KW - Borrelia burgdorferi

KW - co-immunoprecipitation

KW - Lyme disease

KW - RNA chaperone

KW - RNA-binding protein

KW - Borrelia burgdorferi/metabolism

KW - RNA, Bacterial/metabolism

KW - RNA, Messenger/metabolism

KW - RNA-Binding Proteins/metabolism

KW - Bacterial Proteins/metabolism

KW - Lyme Disease/microbiology

KW - Molecular Chaperones/metabolism

KW - Protein Binding

KW - Gene Expression Regulation, Bacterial

UR - https://www.scopus.com/pages/publications/105042320331

U2 - 10.1080/15476286.2026.2684395

DO - 10.1080/15476286.2026.2684395

M3 - Article

C2 - 42233734

AN - SCOPUS:105042320331

SN - 1547-6286

VL - 23

SP - 1

EP - 23

JO - RNA Biology

JF - RNA Biology

IS - 1

ER -

Identification of proteins exhibiting in vitro RNA chaperone activity through gradient profiling in the Lyme disease spirochete, Borrelia burgdorferi

Abstract

Keywords

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