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. 1996 Dec;64(12):5008–5014. doi: 10.1128/iai.64.12.5008-5014.1996

Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae.

C J Chen 1, P F Sparling 1, L A Lewis 1, D W Dyer 1, C Elkins 1
PMCID: PMC174481  PMID: 8945539

Abstract

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.

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Selected References

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