Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae
| Autor: | Lisa A. Lewis, P F Sparling, D W Dyer, Christopher Elkins, C J Chen |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
education.field_of_study
Hemeprotein Binding protein Immunology Population Biology medicine.disease_cause Microbiology Neisseria gonorrhoeae Hemoglobins chemistry.chemical_compound Infectious Diseases Biochemistry chemistry medicine Parasitology Hemoglobin Bacterial outer membrane education Peptide sequence Heme Bacterial Outer Membrane Proteins Protein Binding Research Article |
| Zdroj: | Infection and Immunity. 64:5008-5014 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.64.12.5008-5014.1996 |
| Popis: | The majority of in vitro-grown Neisseria gonorrhoeae strains were unable to use hemoglobin as the sole source of iron for growth (Hgb-), but a minor population was able to do so (Hgb+). The ability of Hgb+ gonococci to utilize hemoglobin as the iron source was associated with the expression of an iron-repressible 89-kDa hemoglobin-binding protein in the outer membrane. The N-terminal amino acid sequence of this protein revealed amino acids, from positions 2 to 16, identical to those of HpuB, an 85 kDa iron-regulated hemoglobin-haptoglobin utilization outer membrane protein of Neisseria meningitidis. Isogenic mutants constructed by allelic replacement with a meningococcal hpu::mini-Tn3erm construct no longer expressed the 89-kDa protein. Mutants could not utilize hemoglobin to support growth but still grew on heme. Thus, the gonococcal HpuB homolog is a functional hemoglobin receptor and is essential for growth with hemoglobin. |
| Databáze: | OpenAIRE |
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