Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae
Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae
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DOI：
10.1128/iai.64.12.5008-5014.1996
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发表时间：
1996-12-01
影响因子：
3.1
通讯作者：
Elkins, C
中科院分区：
文献类型：
--
作者：
Chen, CJ;Sparling, PF;Elkins, C
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.
