Antibodies to ospB prevent infection of C3H mice challenged with Borrelia burgdorferi isolates expressing truncated OspB antigens

William Scott Probert, Melissa Crawford, Rance B Lefebvre

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Truncation of outer surface protein B (OspB) of the Lyme disease agent, Borrelia burgdorferi, may allow the organism to escape immunological destruction and render an OspB-based vaccine ineffective. To investigate this possibility, we have identified two isolates, 297 and CA4, which predominantly express a truncated form of the OspB antigen. In each case, nucleic acid sequencing revealed that truncation of the OspB antigen resulted from a nonsense mutation within the 3' end of the ospB gene. Growth inhibition and protection studies demonstrated that both isolates were neutralized by an anti-OspB serum. Our results indicate that truncated forms of the OspB antigen possess epitopes that may represent important targets for neutralizing antibodies and thus, support the inclusion of OspB as a component of a subunit vaccine.

Original languageEnglish (US)
Pages (from-to)15-19
Number of pages5
JournalVaccine
Volume15
Issue number1
DOIs
StatePublished - Jan 1997

Fingerprint

Borrelia burgdorferi
Inbred C3H Mouse
surface proteins
Membrane Proteins
antigens
Antigens
antibodies
Antibodies
mice
Infection
infection
nonsense mutation
Subunit Vaccines
Lyme disease
Lyme Disease
Nonsense Codon
subunit vaccines
IgA receptor
Neutralizing Antibodies
neutralizing antibodies

Keywords

  • Borrelia burgdorferi
  • outer surface protein
  • vaccine

ASJC Scopus subject areas

  • Immunology
  • Microbiology
  • Virology
  • Infectious Diseases
  • Public Health, Environmental and Occupational Health
  • veterinary(all)

Cite this

Antibodies to ospB prevent infection of C3H mice challenged with Borrelia burgdorferi isolates expressing truncated OspB antigens. / Probert, William Scott; Crawford, Melissa; Lefebvre, Rance B.

In: Vaccine, Vol. 15, No. 1, 01.1997, p. 15-19.

Research output: Contribution to journalArticle

@article{f6fe9d6705a04b8aaf6dd1eb1df07683,
title = "Antibodies to ospB prevent infection of C3H mice challenged with Borrelia burgdorferi isolates expressing truncated OspB antigens",
abstract = "Truncation of outer surface protein B (OspB) of the Lyme disease agent, Borrelia burgdorferi, may allow the organism to escape immunological destruction and render an OspB-based vaccine ineffective. To investigate this possibility, we have identified two isolates, 297 and CA4, which predominantly express a truncated form of the OspB antigen. In each case, nucleic acid sequencing revealed that truncation of the OspB antigen resulted from a nonsense mutation within the 3' end of the ospB gene. Growth inhibition and protection studies demonstrated that both isolates were neutralized by an anti-OspB serum. Our results indicate that truncated forms of the OspB antigen possess epitopes that may represent important targets for neutralizing antibodies and thus, support the inclusion of OspB as a component of a subunit vaccine.",
keywords = "Borrelia burgdorferi, outer surface protein, vaccine",
author = "Probert, {William Scott} and Melissa Crawford and Lefebvre, {Rance B}",
year = "1997",
month = "1",
doi = "10.1016/S0264-410X(96)00123-5",
language = "English (US)",
volume = "15",
pages = "15--19",
journal = "Vaccine",
issn = "0264-410X",
publisher = "Elsevier BV",
number = "1",

}

TY - JOUR

T1 - Antibodies to ospB prevent infection of C3H mice challenged with Borrelia burgdorferi isolates expressing truncated OspB antigens

AU - Probert, William Scott

AU - Crawford, Melissa

AU - Lefebvre, Rance B

PY - 1997/1

Y1 - 1997/1

N2 - Truncation of outer surface protein B (OspB) of the Lyme disease agent, Borrelia burgdorferi, may allow the organism to escape immunological destruction and render an OspB-based vaccine ineffective. To investigate this possibility, we have identified two isolates, 297 and CA4, which predominantly express a truncated form of the OspB antigen. In each case, nucleic acid sequencing revealed that truncation of the OspB antigen resulted from a nonsense mutation within the 3' end of the ospB gene. Growth inhibition and protection studies demonstrated that both isolates were neutralized by an anti-OspB serum. Our results indicate that truncated forms of the OspB antigen possess epitopes that may represent important targets for neutralizing antibodies and thus, support the inclusion of OspB as a component of a subunit vaccine.

AB - Truncation of outer surface protein B (OspB) of the Lyme disease agent, Borrelia burgdorferi, may allow the organism to escape immunological destruction and render an OspB-based vaccine ineffective. To investigate this possibility, we have identified two isolates, 297 and CA4, which predominantly express a truncated form of the OspB antigen. In each case, nucleic acid sequencing revealed that truncation of the OspB antigen resulted from a nonsense mutation within the 3' end of the ospB gene. Growth inhibition and protection studies demonstrated that both isolates were neutralized by an anti-OspB serum. Our results indicate that truncated forms of the OspB antigen possess epitopes that may represent important targets for neutralizing antibodies and thus, support the inclusion of OspB as a component of a subunit vaccine.

KW - Borrelia burgdorferi

KW - outer surface protein

KW - vaccine

UR - http://www.scopus.com/inward/record.url?scp=0031027776&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031027776&partnerID=8YFLogxK

U2 - 10.1016/S0264-410X(96)00123-5

DO - 10.1016/S0264-410X(96)00123-5

M3 - Article

VL - 15

SP - 15

EP - 19

JO - Vaccine

JF - Vaccine

SN - 0264-410X

IS - 1

ER -