Surface exposure and protease insensitivity of Borrelia burgdorferi Erp (OspEF-related) lipoproteins

N. El-Hage; K. Babb; J. A. Carroll; N. Lindstrom; E. R. Fischer; J. C. Miller; Jr Gilmore; M. L. Mbow; B. Stevenson

doi:10.1099/00221287-147-4-821

Surface exposure and protease insensitivity of Borrelia burgdorferi Erp (OspEF-related) lipoproteins

N. El-Hage, K. Babb, J. A. Carroll, N. Lindstrom, E. R. Fischer, J. C. Miller, Jr Gilmore, M. L. Mbow, B. Stevenson

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

62 Scopus citations

Abstract

Borrelia burgdorferi can encode numerous lipoproteins of the Erp family. Although initially described as outer surface proteins, the technique used in that earlier study has since been demonstrated to disrupt bacterial membranes and allow labelling of subsurface proteins. Data are now presented from additional analyses indicating that Erp proteins are indeed surface exposed in the outer membrane. Surface localization of these infection-associated proteins indicates the potential for interactions of Erp proteins with vertebrate tissues. Some Erp proteins were resistant to in situ digestion by certain proteases, suggesting that those proteins fold in manners which hide protease cleavage sites, or that they interact with other protective membrane components. Additionally, cultivation of B. burgdorferi in the presence of antibodies directed against Erp proteins inhibited bacterial growth.

Original language	English
Pages (from-to)	821-830
Number of pages	10
Journal	Microbiology
Volume	147
Issue number	4
DOIs	https://doi.org/10.1099/00221287-147-4-821
State	Published - 2001

Keywords

Bacterial surface proteins
Erp proteins
Immunofluourescence
Lyme disease
Protease resistance
Spirochaete

ASJC Scopus subject areas

Microbiology

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10.1099/00221287-147-4-821

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title = "Surface exposure and protease insensitivity of Borrelia burgdorferi Erp (OspEF-related) lipoproteins",

abstract = "Borrelia burgdorferi can encode numerous lipoproteins of the Erp family. Although initially described as outer surface proteins, the technique used in that earlier study has since been demonstrated to disrupt bacterial membranes and allow labelling of subsurface proteins. Data are now presented from additional analyses indicating that Erp proteins are indeed surface exposed in the outer membrane. Surface localization of these infection-associated proteins indicates the potential for interactions of Erp proteins with vertebrate tissues. Some Erp proteins were resistant to in situ digestion by certain proteases, suggesting that those proteins fold in manners which hide protease cleavage sites, or that they interact with other protective membrane components. Additionally, cultivation of B. burgdorferi in the presence of antibodies directed against Erp proteins inhibited bacterial growth.",

keywords = "Bacterial surface proteins, Erp proteins, Immunofluourescence, Lyme disease, Protease resistance, Spirochaete",

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T1 - Surface exposure and protease insensitivity of Borrelia burgdorferi Erp (OspEF-related) lipoproteins

AU - El-Hage, N.

AU - Babb, K.

AU - Carroll, J. A.

AU - Lindstrom, N.

AU - Fischer, E. R.

AU - Miller, J. C.

AU - Gilmore, Jr

AU - Mbow, M. L.

AU - Stevenson, B.

PY - 2001

Y1 - 2001

N2 - Borrelia burgdorferi can encode numerous lipoproteins of the Erp family. Although initially described as outer surface proteins, the technique used in that earlier study has since been demonstrated to disrupt bacterial membranes and allow labelling of subsurface proteins. Data are now presented from additional analyses indicating that Erp proteins are indeed surface exposed in the outer membrane. Surface localization of these infection-associated proteins indicates the potential for interactions of Erp proteins with vertebrate tissues. Some Erp proteins were resistant to in situ digestion by certain proteases, suggesting that those proteins fold in manners which hide protease cleavage sites, or that they interact with other protective membrane components. Additionally, cultivation of B. burgdorferi in the presence of antibodies directed against Erp proteins inhibited bacterial growth.

AB - Borrelia burgdorferi can encode numerous lipoproteins of the Erp family. Although initially described as outer surface proteins, the technique used in that earlier study has since been demonstrated to disrupt bacterial membranes and allow labelling of subsurface proteins. Data are now presented from additional analyses indicating that Erp proteins are indeed surface exposed in the outer membrane. Surface localization of these infection-associated proteins indicates the potential for interactions of Erp proteins with vertebrate tissues. Some Erp proteins were resistant to in situ digestion by certain proteases, suggesting that those proteins fold in manners which hide protease cleavage sites, or that they interact with other protective membrane components. Additionally, cultivation of B. burgdorferi in the presence of antibodies directed against Erp proteins inhibited bacterial growth.

KW - Bacterial surface proteins

KW - Erp proteins

KW - Immunofluourescence

KW - Lyme disease

KW - Protease resistance

KW - Spirochaete

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DO - 10.1099/00221287-147-4-821

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JO - Microbiology

JF - Microbiology

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ER -

Surface exposure and protease insensitivity of Borrelia burgdorferi Erp (OspEF-related) lipoproteins

Abstract

Keywords

ASJC Scopus subject areas

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