Infect Immun, March 1998, p. 987-993, Vol. 66, No. 3
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Departments of Medicine1 and Microbiology and Immunology,2 School of Medicine, University of North Carolina, Chapel Hill, North Carolina 27599
Received 8 October 1997/Returned for modification 10 December 1997/Accepted 30 December 1997
Most Neisseria gonorrhoeae isolates are unable to use
human hemoglobin as the sole source of iron for growth
(Hgb
), but a minor population is able to do so
(Hgb+). This minor population grows luxuriously on
hemoglobin, expresses two outer membrane proteins of 42 kDa (HpuA) and
89 kDa (HpuB), and binds hemoglobin under iron-stressed conditions. In
addition to the previously reported HpuB, we identified and
characterized HpuA, which is encoded by the gene hpuA,
located immediately upstream of hpuB. Expression of both
proteins was found to be controlled at the translational level by
frameshift mutations in a run of guanine residues within the
hpuA sequence encoding the mature HpuA protein. The
"on-phase" hemoglobin-utilizing variants contained 10 G's, while
the "off-phase" variants contained 9 G's. Insertional hpuB mutants of FA19 Hgb+ and FA1090
Hgb+ no longer expressed HpuB but still produced HpuA. A
polar insertional mutation of the upstream hpuA gene in
FA1090 Hgb+ eliminated production of both HpuA and HpuB,
whereas a nonpolar insertional mutant expressed HpuB only. Insertional
mutagenesis of either hpuA or hpuB or both
substantially decreased the hemoglobin binding ability of the FA1090
Hgb+ variant and prevented growth on hemoglobin plates.
Therefore, both HpuA and HpuB were required for the utilization of
hemoglobin for growth.
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