Characterization of lbpA, the structural gene for a lactoferrin receptor in Neisseria gonorrhoeae
| Autor: | G D Biswas, P F Sparling |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
DNA
Bacterial Molecular Sequence Data Restriction Mapping Immunology Mutant Receptors Cell Surface Transferrin receptor medicine.disease_cause Microbiology medicine Amino Acid Sequence Gene Base Sequence Sequence Homology Amino Acid biology Lactoferrin Structural gene biology.organism_classification Molecular biology Neisseria gonorrhoeae Infectious Diseases Genes Bacterial Mutagenesis DNA Transposable Elements biology.protein Parasitology Neisseriaceae Bacterial outer membrane Sequence Alignment Research Article Bacterial Outer Membrane Proteins |
| Zdroj: | Infection and Immunity. 63:2958-2967 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.63.8.2958-2967.1995 |
| Popis: | Neisseria gonorrhoeae acquires iron (Fe) efficiently from lactoferrin (LF). A 103-kDa gonococcal outer membrane LF-binding protein (Lbp) was identified previously. We isolated the structural gene lbpA for Lbp1 by screening a gonococcal library for a clone that could repair an LF- receptor mutant. An mTnCm3 transposon insertion mutant of lbpA was unable to use LF-bound Fe for growth, unable to bind LF to whole cells, and unable to express Lbp1. The DNA sequence of lbpA predicted a protein that shared 94% identity with the meningococcal LF receptor protein, Lbp, and was closely related to Tbp1, one of the transferrin receptor proteins. Clinical isolates of gonococci are frequently unable to acquire Fe from LF, and LF- isolates do not have a functional LF receptor. The wild-type lbpA gene transformed most tested LF- clinical isolates to LF+, indicating that lbpA is defective in many clinical isolates. |
| Databáze: | OpenAIRE |
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