PMID- 10024553
OWN - NLM
STAT- MEDLINE
DCOM- 19990312
LR  - 20200724
IS  - 0019-9567 (Print)
IS  - 1098-5522 (Electronic)
IS  - 0019-9567 (Linking)
VI  - 67
IP  - 3
DP  - 1999 Mar
TI  - Identification and characterization of a novel Ibe10 binding protein that 
      contributes to Escherichia coli invasion of brain microvascular endothelial 
      cells.
PG  - 1131-8
AB  - The molecular basis of Escherichia coli traversal of the blood-brain barrier in 
      the development of E. coli meningitis is not well understood. We have previously 
      shown that a novel Ibe10 protein found in cerebrospinal fluid isolates of E. coli 
      is necessary for invasion of the brain microvascular endothelial cells (BMEC) 
      that constitute the blood-brain barrier both in vitro and in a newborn rat model 
      of hematogenous meningitis. Here we identified a novel Ibe10 binding 
      molecule/receptor (Ibe10R) on both bovine BMEC (HBMEC) and human BMEC (HBMEC) 
      that is responsible for invasion by E. coli. Ibe10R, an approximately 55-kDa 
      protein, was purified from BBMEC by Ibe10-Ni-Sepharose affinity chromatography. 
      Bovine Ibe10R, as well as polyclonal antibodies to Ibe10R, blocked E. coli 
      invasion of BBMEC very effectively. The N-terminal amino acid sequence of Ibe10R 
      showed 75% homology to serum albumin. However, the amino acid sequence of an 
      Ibe10R fragment generated by limited enzymatic digestion did not reveal homology 
      to any other proteins, suggesting that Ibe10R represents a novel albumin-like 
      protein. Immunocytochemical analysis of BBMEC using anti-Ibe10R antibody 
      suggested that only a subset of cultured BBMEC express Ibe10R on their surface. 
      Enrichment of Ibe10R-positive BBMEC by fluorescence-activated cell sorting with 
      anti-Ibe10R antibody resulted in enhanced invasion by E. coli. The anti-Ibe10R 
      antibody raised against bovine Ibe10R also blocked E. coli invasion of HBMEC very 
      effectively. Interestingly, anti-Ibe10R antibody affinity chromatography of HBMEC 
      membrane proteins revealed a smaller protein with an approximate molecular mass 
      of 45 kDa. These results suggest that the Ibe10 of E. coli interacts with a novel 
      BMEC surface protein, Ibe10R, for invasion of both BBMEC and HBMEC.
FAU - Prasadarao, N V
AU  - Prasadarao NV
AD  - Division of Infectious Diseases, Childrens Hospital Los Angeles, and University 
      of Southern California School of Medicine, Los Angeles, California 90027, 
      USA.nemani@hsc.usc.edu
FAU - Wass, C A
AU  - Wass CA
FAU - Huang, S H
AU  - Huang SH
FAU - Kim, K S
AU  - Kim KS
LA  - eng
GR  - R29 AI040635/AI/NIAID NIH HHS/United States
GR  - R01-NS26310/NS/NINDS NIH HHS/United States
GR  - R29-AI40567/AI/NIAID NIH HHS/United States
GR  - R29-AI40635/AI/NIAID NIH HHS/United States
GR  - R29 AI040567/AI/NIAID NIH HHS/United States
GR  - R01 NS026310/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Bacterial Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (CusC protein, E coli)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Membrane Proteins)
SB  - IM
MH  - Animals
MH  - Bacterial Proteins/*physiology
MH  - Brain/*microbiology
MH  - Carrier Proteins/analysis/*physiology
MH  - Cattle
MH  - Endothelium, Vascular/*microbiology
MH  - Escherichia coli/*pathogenicity
MH  - *Escherichia coli Proteins
MH  - Humans
MH  - Infant, Newborn
MH  - Membrane Proteins/*physiology
MH  - Rats
PMC - PMC96439
EDAT- 1999/02/20 00:00
MHDA- 1999/02/20 00:01
PMCR- 1999/03/01
CRDT- 1999/02/20 00:00
PHST- 1999/02/20 00:00 [pubmed]
PHST- 1999/02/20 00:01 [medline]
PHST- 1999/02/20 00:00 [entrez]
PHST- 1999/03/01 00:00 [pmc-release]
AID - 1246 [pii]
AID - 10.1128/IAI.67.3.1131-1138.1999 [doi]
PST - ppublish
SO  - Infect Immun. 1999 Mar;67(3):1131-8. doi: 10.1128/IAI.67.3.1131-1138.1999.