The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells

G. R. Bolduc, M. J. Baron, Claudia Gravekamp, C. S. Lachenauer, L. C. Madoff

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Group B Streptococcus (GBS) is the leading cause of bacterial chorioamnionitis and neonatal pneumonia, sepsis, and meningitis. Deletion of the alpha C protein gene (bca) attenuates the virulence of GBS in an animal model; significant survival differences in the first 24 h of infection suggest a pathogenic role for the alpha C protein early in the infection process. We examined the role of alpha C protein in the association between GBS and mucosal surfaces using a human cervical epithelial cell line, ME180. Fluorescent and confocal microscopy and flow cytometry demonstrated that 9-repeat alpha C protein binds to the surface of ME180 cells. Isolated N-terminal region of this protein also binds to these cells and competitively inhibits binding of the full protein. Wild-type GBS strain A909 and the bca-null isogenic mutant JL2053 bound similarly to the surface of ME180 cells. However, A909 entered these cells threefold more. Internalization of A909 was inhibited with 2- and 9-repeat alpha C and with N-terminal region alone but not by repeat region-specific peptide. Translocation across polarized ME180 membranes was fivefold greater for A909 than for JL2053. These findings suggest a role for the alpha C protein in interaction with epithelial surfaces and initiation of infection.

Original languageEnglish (US)
Pages (from-to)751-758
Number of pages8
JournalCellular Microbiology
Volume4
Issue number11
DOIs
StatePublished - Nov 1 2002
Externally publishedYes

Fingerprint

Streptococcus agalactiae
Protein C
Epithelial Cells
Infection
Chorioamnionitis
Proteins
Flow cytometry
Confocal microscopy
Meningitis
Confocal Microscopy
Virulence
Pneumonia
Carrier Proteins
Flow Cytometry
Animals
Animal Models
Membranes
Cell Line
Peptides
Survival

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Microbiology

Cite this

The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells. / Bolduc, G. R.; Baron, M. J.; Gravekamp, Claudia; Lachenauer, C. S.; Madoff, L. C.

In: Cellular Microbiology, Vol. 4, No. 11, 01.11.2002, p. 751-758.

Research output: Contribution to journalArticle

Bolduc, G. R. ; Baron, M. J. ; Gravekamp, Claudia ; Lachenauer, C. S. ; Madoff, L. C. / The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells. In: Cellular Microbiology. 2002 ; Vol. 4, No. 11. pp. 751-758.
@article{7b9470755442440998cdd98163ec0f0d,
title = "The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells",
abstract = "Group B Streptococcus (GBS) is the leading cause of bacterial chorioamnionitis and neonatal pneumonia, sepsis, and meningitis. Deletion of the alpha C protein gene (bca) attenuates the virulence of GBS in an animal model; significant survival differences in the first 24 h of infection suggest a pathogenic role for the alpha C protein early in the infection process. We examined the role of alpha C protein in the association between GBS and mucosal surfaces using a human cervical epithelial cell line, ME180. Fluorescent and confocal microscopy and flow cytometry demonstrated that 9-repeat alpha C protein binds to the surface of ME180 cells. Isolated N-terminal region of this protein also binds to these cells and competitively inhibits binding of the full protein. Wild-type GBS strain A909 and the bca-null isogenic mutant JL2053 bound similarly to the surface of ME180 cells. However, A909 entered these cells threefold more. Internalization of A909 was inhibited with 2- and 9-repeat alpha C and with N-terminal region alone but not by repeat region-specific peptide. Translocation across polarized ME180 membranes was fivefold greater for A909 than for JL2053. These findings suggest a role for the alpha C protein in interaction with epithelial surfaces and initiation of infection.",
author = "Bolduc, {G. R.} and Baron, {M. J.} and Claudia Gravekamp and Lachenauer, {C. S.} and Madoff, {L. C.}",
year = "2002",
month = "11",
day = "1",
doi = "10.1046/j.1462-5822.2002.00227.x",
language = "English (US)",
volume = "4",
pages = "751--758",
journal = "Cellular Microbiology",
issn = "1462-5814",
publisher = "Wiley-Blackwell",
number = "11",

}

TY - JOUR

T1 - The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells

AU - Bolduc, G. R.

AU - Baron, M. J.

AU - Gravekamp, Claudia

AU - Lachenauer, C. S.

AU - Madoff, L. C.

PY - 2002/11/1

Y1 - 2002/11/1

N2 - Group B Streptococcus (GBS) is the leading cause of bacterial chorioamnionitis and neonatal pneumonia, sepsis, and meningitis. Deletion of the alpha C protein gene (bca) attenuates the virulence of GBS in an animal model; significant survival differences in the first 24 h of infection suggest a pathogenic role for the alpha C protein early in the infection process. We examined the role of alpha C protein in the association between GBS and mucosal surfaces using a human cervical epithelial cell line, ME180. Fluorescent and confocal microscopy and flow cytometry demonstrated that 9-repeat alpha C protein binds to the surface of ME180 cells. Isolated N-terminal region of this protein also binds to these cells and competitively inhibits binding of the full protein. Wild-type GBS strain A909 and the bca-null isogenic mutant JL2053 bound similarly to the surface of ME180 cells. However, A909 entered these cells threefold more. Internalization of A909 was inhibited with 2- and 9-repeat alpha C and with N-terminal region alone but not by repeat region-specific peptide. Translocation across polarized ME180 membranes was fivefold greater for A909 than for JL2053. These findings suggest a role for the alpha C protein in interaction with epithelial surfaces and initiation of infection.

AB - Group B Streptococcus (GBS) is the leading cause of bacterial chorioamnionitis and neonatal pneumonia, sepsis, and meningitis. Deletion of the alpha C protein gene (bca) attenuates the virulence of GBS in an animal model; significant survival differences in the first 24 h of infection suggest a pathogenic role for the alpha C protein early in the infection process. We examined the role of alpha C protein in the association between GBS and mucosal surfaces using a human cervical epithelial cell line, ME180. Fluorescent and confocal microscopy and flow cytometry demonstrated that 9-repeat alpha C protein binds to the surface of ME180 cells. Isolated N-terminal region of this protein also binds to these cells and competitively inhibits binding of the full protein. Wild-type GBS strain A909 and the bca-null isogenic mutant JL2053 bound similarly to the surface of ME180 cells. However, A909 entered these cells threefold more. Internalization of A909 was inhibited with 2- and 9-repeat alpha C and with N-terminal region alone but not by repeat region-specific peptide. Translocation across polarized ME180 membranes was fivefold greater for A909 than for JL2053. These findings suggest a role for the alpha C protein in interaction with epithelial surfaces and initiation of infection.

UR - http://www.scopus.com/inward/record.url?scp=0036854515&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036854515&partnerID=8YFLogxK

U2 - 10.1046/j.1462-5822.2002.00227.x

DO - 10.1046/j.1462-5822.2002.00227.x

M3 - Article

VL - 4

SP - 751

EP - 758

JO - Cellular Microbiology

JF - Cellular Microbiology

SN - 1462-5814

IS - 11

ER -