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Characterization of Pit, a Streptococcus pneumoniae Iron Uptake ABC Transporter
- Source :
- Infection and Immunity. 70:4389-4398
- Publication Year :
- 2002
- Publisher :
- American Society for Microbiology, 2002.
-
Abstract
- Bacteria frequently have multiple mechanisms for acquiring iron, an essential micronutrient, from the environment. We have identified a four-gene Streptococcus pneumoniae operon, named pit , encoding proteins with similarity to components of a putative Brachyspira hyodysenteriae iron uptake ABC transporter, Bit. An S. pneumoniae strain containing a defined mutation in pit has impaired growth in medium containing the iron chelator ethylenediamine di- o -hydroxyphenylacetic acid, reduced sensitivity to the iron-dependent antibiotic streptonigrin, and impaired virulence in a mouse model of S. pneumoniae systemic infection. Furthermore, addition of a mutation in pit to a strain containing mutations in the two previously described S. pneumoniae iron uptake ABC transporters, piu and pia , resulted in a strain with impaired growth in two types of iron-deficient medium, a high degree of resistance to streptonigrin, and a reduced rate of iron uptake. Comparison of the susceptibilities to streptonigrin of the individual pit , piu , and pia mutant strains and comparison of the growth in iron-deficient medium and virulence of single and double mutant strains suggest that pia is the dominant iron transporter during in vitro and in vivo growth.
- Subjects :
- Transcription, Genetic
Operon
Iron
Immunology
Mutant
Virulence
ATP-binding cassette transporter
Biology
medicine.disease_cause
Ferric Compounds
Microbiology
chemistry.chemical_compound
Bacterial Proteins
Chlorides
Iron-Binding Proteins
Streptococcus pneumoniae
medicine
Streptonigrin
Errata
Iron-binding proteins
Gene Expression Regulation, Bacterial
Sequence Analysis, DNA
biology.organism_classification
Molecular Pathogenesis
Culture Media
Infectious Diseases
chemistry
Mutagenesis
Periplasmic Binding Proteins
ATP-Binding Cassette Transporters
Parasitology
Bacteria
Bacterial Outer Membrane Proteins
Subjects
Details
- ISSN :
- 10985522 and 00199567
- Volume :
- 70
- Database :
- OpenAIRE
- Journal :
- Infection and Immunity
- Accession number :
- edsair.doi.dedup.....a87a5f9f4a9f21534d914028ea36eb5a
- Full Text :
- https://doi.org/10.1128/iai.70.8.4389-4398.2002