Chapter 17 : Neisseria

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $15.00

Preview this chapter:
Zoom in

Neisseria, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555816544/9781555812928_Chap17-1.gif /docserver/preview/fulltext/10.1128/9781555816544/9781555812928_Chap17-2.gif


The genus consists of two human pathogens, (gonococcus) and (meningococcus), as well as several commensal species, including . Although the pathogenic species are considered classical extracellular pathogens, intraepithelial cell growth was documented recently, and it is possible that invasion of and growth within host cells plays an important role in pathogenesis. The pathogenic species express a wide array of iron acquisition systems. Although the species are not known to synthesize or secrete detectable siderophores, they are capable of iron acquisition from host transferrin, lactoferrin, and hemoglobin without the synthesis of a siderophore intermediate. Iron acquisition from these host proteins occurs via a process that is dependent on the expression of specific outer membrane receptors. In addition to these sources of iron, the pathogenic species are capable of using heme, siderophores made by other microorganisms (xenosiderophores), and a variety of keto acid-iron complexes as sole iron sources.

Citation: Nau Cornelissen C, Sparling P. 2004. Neisseria, p 256-272. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch17

Key Concept Ranking

Outer Membrane Proteins
Sodium Dodecyl Sulfate
Pelvic Inflammatory Disease
Integral Membrane Proteins
Highlighted Text: Show | Hide
Loading full text...

Full text loading...


Image of FIGURE 1

Model of iron acquisition systems expressed by the species. TbpA and TbpB are outer membrane (OM) proteins that bind to transferrin and subsequently facilitate iron removal and internalization. LbpA and LbpB are similar proteins that function as the lactoferrin receptor. HpuA and HpuB are homologous to the Tbp and Lbp receptor proteins and facilitate the utilization of hemoglobin as a heme and iron source. Another hemoglobin receptor, HmbR (not shown), is expressed by and does not conform to this two-protein receptor paradigm, as discussed in the text. FbpA is a periplasmic (PP), protein and FbpB and FbpC are shown as integral cytoplasmic membrane (CM) proteins. This group of proteins facilitates the periplasmic and cytoplasmic transport of iron, donated by transferrin or lactoferrin. The TonB, ExbB, and ExbD energy transduction system is shown within or tethered to the cytoplasmic membrane. This group of proteins is required for energization of all three iron acquisition systems shown. See the text for details.

Citation: Nau Cornelissen C, Sparling P. 2004. Neisseria, p 256-272. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch17
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of FIGURE 2

Genetic arrangement of genes. By comparison with the genes, encoding the lactoferrin receptor, and with the genes, encoding the hemoglobin receptor, only the genes are separated by an intergenic region. This region consists of 86 bp and includes a region of dyad symmetry (arrows) capable of forming a stem-loop structure in mRNA. The promoter region that precedes is also shown; it includes canonical promoter, overlapped by a putative Fur binding site (Fur box). The transcriptional start site, ribosome start site (RBS), and start codon are also shown.

Citation: Nau Cornelissen C, Sparling P. 2004. Neisseria, p 256-272. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch17
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of FIGURE 3

Naturally occurring mutations in . Two major classes of mutants have been characterized that result in no expression of the LbpB protein. (A) A polypyrimidine tract consisting of 10 C residues results in expression of the LbpB protein, while a decrease in the number of C residues to 8 or 9 shifts the gene out of frame and prevents LbpB expression. Expression is found with C strings of 7 or 13 residues as well. (B) A deletion of 2.7 kb with a concomitant insertion of 41 residues of a repeated element (black box) results in a gene fusion between the upstream gene, which encodes a GTP-binding protein, and the gene. This fusion event results in no expression of either LbpB or LbpA. Not shown are various point mutations in or , which also result in loss of expression in some isolates. P indicates the approximate position of the iron-regulated promoter that drives the expression of .

Citation: Nau Cornelissen C, Sparling P. 2004. Neisseria, p 256-272. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch17
Permissions and Reprints Request Permissions
Download as Powerpoint


1. Adhikari, P.,, S. A. Berish,, A. J. Nowalk,, K. L. Veraldi,, S. A. Morse,, and T. A. Mietzner. 1996. The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron. J. Bacteriol. 178:21452149.
2. Anderson, J. E.,, M. M. Hobbs,, G. D. Biswas,, and P. F. Sparling. 2003. Opposing selective forces for expression of the gonococcal lactoferrin receptor. Mol. Microbiol. 48:13251337.
3. Bayliss, C. D.,, D. Field,, and E. R. Moxon. 2001. The simple contingency loci of Haemophilus influenzae and Neisseria meningitidis. J. Clin. Investig. 107: 657662.
4. Boulton, I. C.,, M. K. Yost,, J. E. Anderson,, and C. N. Cornelissen. 2000. Identification of discrete domains within gonococcal transferrin-binding protein A that are necessary for ligand binding and iron uptake functions. Infect. Immun. 68:69886996.
5. Carson, S. D.,, B. Stone,, M. Beucher,, J. Fu,, and P. F. Sparling. 2000. Phase variation of the gonococcal siderophore receptor FetA. Mol. Microbiol. 36: 585593.
6. Carson, S. D. B.,, P. E. Klebba,, S. M. C. Newton,, and P. F. Sparling. 1999. Ferric enterobactin binding and utilization by Neisseria gonorrhoeae. J. Bacteriol. 181:28952901.
7. Chen, C. J.,, D. Mclean,, C. E. Thomas,, J. E. Anderson,, and P. F. Sparling. 2002. Point mutations in HpuB enable gonococcal HpuA deletion mutants to grow on hemoglobin. J. Bacteriol. 184:420426.
8. Cohen, M. S.,, and J. G. Cannon. 1999. Human experimentation with Neisseria gonorrhoeae: progress and goals. J. Infect. Dis. 179:S375S379.
9. Cornelissen, C. N.,, J. E. Anderson,, and P. F. Sparling. 1997. Energy-dependent changes in the gonococcal transferrin receptor. Mol. Microbiol. 26: 2535.
10. Cornelissen, C. N.,, M. Kelley,, M. M. Hobbs,, J. E. Anderson,, J. G. Cannon,, M. S. Cohen,, and P. F. Sparling. 1998. The transferrin receptor expressed by gonococcal strain FA1090 is required for the experimental infection of human male volunteers. Mol. Microbiol. 27:611616.
11. Dehio, C.,, S. D. Gray-Owen,, and T. F. Meyer. 1998. The role of neisserial Opa proteins in interactions with host cells. Trends Microbiol. 6:489495.
12. Jerse, A. E.,, E. T. Crow,, A. N. Bordner,, I. Rahman,, C. N. Cornelissen,, T. R. Moench,, and K. Mehrazar. 2002. Growth of Neisseria gonorrhoeae in the female mouse genital tract does not require the gonococcal transferrin or hemoglobin receptors and may be enhanced by commensal lactobacilli. Infect. Immun. 70:25492558.
13. Kenney, C. D.,, and C. N. Cornelissen. 2002. Demonstration and characterization of a specific in teraction between gonococcal transferrin binding protein A and TonB. J. Bacteriol. 184:61386145.
14. Klee, S. R.,, X. Nassif,, B. Kusecek,, P. Merker,, J.-L. Beretti,, M. Achtman,, and C. R. Tinsley. 2000. Molecular and biological analysis of eight genetic islands that distinguish Neisseria meningitidis from the closely related pathogen Neisseria gonorrhoeae. Infect. Immun. 68:20822095.
15. Larson, J. A.,, D. L. Higashi,, I. Stojiljkovic,, and M. So. 2002. Replication of Neisseria meningitidis within epithelial cells requires TonB-dependent acquitision of host cell iron. Infect. Immun. 70: 14611467.
16. Lewis, L. A.,, E. Gray,, Y.-P. Wang,, B. A. Roe,, and D. W. Dyer. 1997. Molecular characterization of hpuAB, the haemoglobin-haptoglobin-utilization operon of Neisseria meningitidis. Mol. Microbiol. 23: 737749.
17. Masri, H. P.,, and C. N. Cornelissen. 2002. Specific ligand binding attributable to individual epitopes of gonococcal transferrin binding protein A. Infect. Immun. 70:732740.
18. Merz, A. J.,, and M. So. 2000. Interactions of pathogenic neisseriae with epithelial cell membranes. Annu. Rev. Cell Dev. Biol. 16:423457.
19. Nassif, X.,, C. Pujol,, P. Morand,, and E. Eugene. 1999. Interactions of pathogenic Neisseria with host cells. Is it possible to assemble the puzzle? Mol. Microbiol. 32:11241132.
20. Ram, S.,, M. Cullinane,, A. M. Blom,, S. Gulati,, D. P. McQuillen,, B. G. Monks,, C. O’Connell,, R. Broden,, C. Elkins,, M. D. Pangburn,, B. Dahlback,, and P. A. Rice. 2001. Binding of C4bbinding protein to porin: a molecular mechanism of serum resistance of Neisseria gonorrhoeae. J. Exp. Med. 193:281295.
21. Ronpirin, C.,, A. E. Jerse,, and C. N. Cornelissen. 2001. The gonococcal genes encoding transferrin binding proteins (Tbp) A and B are arranged in a bicistronic operon but are subject to differential expression. Infect. Immun. 69:63366347.
22. Schryvers, A. B.,, and I. Stojiljkovic. 1999. Iron acquisition systems in the pathogenic Neisseria. Mol. Microbiol. 32:11171123.
23. Turner, P. C.,, C. E. Thomas,, C. Elkins,, S. Clary,, and P. F. Sparling. 1998. Neisseria gonorrhoeae heme biosynthetic mutants utilize heme and hemoglobin as heme sources but fail to grow within epithelial cells. Infect. Immun. 66:52155223.

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error