PMID- 7815944
OWN - NLM
STAT- MEDLINE
DCOM- 19950209
LR  - 20190725
IS  - 0950-382X (Print)
IS  - 0950-382X (Linking)
VI  - 13
IP  - 5
DP  - 1994 Sep
TI  - The 100 kDa haem:haemopexin-binding protein of Haemophilus influenzae: structure 
      and localization.
PG  - 863-73
AB  - All Haemophilus influenzae strains have an absolute requirement for exogenously 
      supplied haem for aerobic growth. A majority of strains of H. influenzae type b 
      (Hib) produce a 100 kDa protein which binds haem: haemopexin complexes. This 100 
      kDa haem:haemopexin binding protein, designated HxuA, was originally detected on 
      the Hib cell surface. Monoclonal antibody (mAb)-based analyses revealed that the 
      HxuA protein was also present in soluble form in Hib culture supernatants. This 
      soluble HxuA protein exhibited haem:haemopexin-binding activity in a direct 
      binding assay. Nucleotide sequence analysis of the hxuA gene from Hib strain 
      DL42, together with N-terminal amino acid analysis of HxuA protein purified from 
      Hib culture supernatant, revealed that this protein was synthesized as a 101 kDa 
      precursor with a leader peptide that was removed to yield a 99 kDa protein. 
      Southern blot analysis of chromosomal DNA from four Hib and four non-typeable H. 
      influenzae (NTHI) strains detected the presence of a single band in each strain 
      that hybridized a Hib hxuA gene probe. Subsequent analysis of these NTHI strains 
      showed that all four strains released into culture supernatant a 
      haem:haemopexin-binding protein that migrated in SDS-PAGE at a rate similar or 
      identical to that of the Hib HxuA protein. A Hib hxuA mutant was used to screen 
      an NTHI genomic DNA library and an NTHI gene was cloned that complemented the 
      mutation in this Hib strain. Nucleotide sequence analysis of this NTHI gene 
      revealed that it encoded a protein with 87% identity to the Hib HxuA 
      protein.(ABSTRACT TRUNCATED AT 250 WORDS)
FAU - Cope, L D
AU  - Cope LD
AD  - Department of Microbiology, University of Texas Southwestern Medical Center, 
      Dallas 75235.
FAU - Thomas, S E
AU  - Thomas SE
FAU - Latimer, J L
AU  - Latimer JL
FAU - Slaughter, C A
AU  - Slaughter CA
FAU - Muller-Eberhard, U
AU  - Muller-Eberhard U
FAU - Hansen, E J
AU  - Hansen EJ
LA  - eng
SI  - GENBANK/U08348
SI  - GENBANK/U08349
GR  - AI-17621/AI/NIAID NIH HHS/United States
GR  - DK-30203/DK/NIDDK NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Mol Microbiol
JT  - Molecular microbiology
JID - 8712028
RN  - 0 (Antibodies, Bacterial)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (heme receptor)
RN  - 42VZT0U6YR (Heme)
RN  - 9013-71-2 (Hemopexin)
SB  - IM
GS  - hxuA
MH  - Amino Acid Sequence
MH  - Antibodies, Bacterial/immunology
MH  - Antibodies, Monoclonal/immunology
MH  - Base Sequence
MH  - Genes, Bacterial
MH  - Haemophilus influenzae/genetics/immunology/*metabolism
MH  - Heme/*metabolism
MH  - Hemopexin/*metabolism
MH  - Molecular Sequence Data
MH  - Receptors, Cell Surface/chemistry/genetics/immunology/*isolation & purification
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
EDAT- 1994/09/01 00:00
MHDA- 1994/09/01 00:01
CRDT- 1994/09/01 00:00
PHST- 1994/09/01 00:00 [pubmed]
PHST- 1994/09/01 00:01 [medline]
PHST- 1994/09/01 00:00 [entrez]
AID - 10.1111/j.1365-2958.1994.tb00478.x [doi]
PST - ppublish
SO  - Mol Microbiol. 1994 Sep;13(5):863-73. doi: 10.1111/j.1365-2958.1994.tb00478.x.