Skip to main content
NCBI home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1980 Nov 1;152(5):1442–1447. doi: 10.1084/jem.152.5.1442

IgA proteases of two distinct specificities are released by Neisseria meningitidis

PMCID: PMC2185987  PMID: 6776228

Abstract

Strains of Neisseria meningitidis produce two distinct extracellular IgA proteases that cleave the human IgA1 heavy chain at different points within the hinge region. Type 1 protease cleaves the prolyl- seryl peptide bond at position 237-238; type type 2 protease cleaves the prolyl-threonyl bond two residues amino terminal to that bond attacked by type 1 enzyme. Each meningococcal isolate elaborates only one of these two enzymes, and the type of protease produced correlates with certain serogroups: group A yielding only type 1, and groups X and Y only type 2 enzyme. In addition, analysis of amino acid sequences of human alpha-chain proteins reveals that the repeating octapeptide characteristic of the IgA1 hinge region is actually triplicated.

Full Text

The Full Text of this article is available as a PDF (577.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Doellgast G. J., Plaut A. G. Purification of human IgA by salt-mediated hydrophobic chromatography. Immunochemistry. 1976 Feb;13(2):135–139. doi: 10.1016/0019-2791(76)90281-0. [DOI] [PubMed] [Google Scholar]
  2. Frangione B., Franklin E. C. Correlation between fragmented immunoglobulin genes and heavy chain deletion mutants. Nature. 1979 Oct 18;281(5732):600–602. doi: 10.1038/281600a0. [DOI] [PubMed] [Google Scholar]
  3. Frangione B., Lee L., Haber E., Bloch K. J. Protein Hal: partial deletion of a " " immunoglobulin gene(s) and apparent reinitiation at an internal AUG codon. Proc Natl Acad Sci U S A. 1973 Apr;70(4):1073–1077. doi: 10.1073/pnas.70.4.1073. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Frangione B., Wolfenstein-Todel C. Partial duplication in the "hinge" region of IgA 1 myeloma proteins. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3673–3676. doi: 10.1073/pnas.69.12.3673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kilian M., Mestecky J., Kulhavy R., Tomana M., Butler W. T. IgA1 proteases from Haemophilus influenzae, Streptococcus pneumoniae, Neisseria meningitidis, and Streptococcus sanguis: comparative immunochemical studies. J Immunol. 1980 Jun;124(6):2596–2600. [PubMed] [Google Scholar]
  6. Kilian M., Mestecky J., Schrohenloher R. E. Pathogenic species of the genus Haemophilus and Streptococcus pneumoniae produce immunoglobulin A1 protease. Infect Immun. 1979 Oct;26(1):143–149. doi: 10.1128/iai.26.1.143-149.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kratzin H., Altevogt P., Ruban E., Kortt A., Staroscik K., Hilschmann N. Die Primärstruktur eines monoklonalen IgA-Immunoglobulins (IgA Tro.), II. Die Aminosäuresequenz der H-Kette, alpha-Typ, Subgruppe III. Struktur des gesamten IgA-Moleküls. Hoppe Seylers Z Physiol Chem. 1975 Aug;356(8):1337–1342. [PubMed] [Google Scholar]
  8. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  9. Lai C. Y. Detection of peptides by fluorescence methods. Methods Enzymol. 1977;47:236–243. doi: 10.1016/0076-6879(77)47028-9. [DOI] [PubMed] [Google Scholar]
  10. Liu Y. S., Low T. L., Infante A., Putnam F. W. Complete covalent structure of a human IgA1 immunoglobulin. Science. 1976 Sep 10;193(4257):1017–1020. doi: 10.1126/science.821146. [DOI] [PubMed] [Google Scholar]
  11. Male C. J. Immunoglobulin A1 protease production by Haemophilus influenzae and Streptococcus pneumoniae. Infect Immun. 1979 Oct;26(1):254–261. doi: 10.1128/iai.26.1.254-261.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Michaelsen T. E., Frangione B., Franklin E. C. Primary structure of the "hinge" region of human IgG3. Probable quadruplication of a 15-amino acid residue basic unit. J Biol Chem. 1977 Feb 10;252(3):883–889. [PubMed] [Google Scholar]
  13. Miyata T., Yasunaga T., Yamawaki-Kataoka Y., Obata M., Honjo T. Nucleotide sequence divergence of mouse immunoglobulin gamma 1 and gamma 2b chain genes and the hypothesis of intervening sequence-mediated domain transfer. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2143–2147. doi: 10.1073/pnas.77.4.2143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mulks M. H., Kornfeld S. J., Plaut A. G. Specific proteolysis of human IgA by Streptococcus pneumoniae and Haemophilus influenzae. J Infect Dis. 1980 Apr;141(4):450–456. doi: 10.1093/infdis/141.4.450. [DOI] [PubMed] [Google Scholar]
  15. Mulks M. H., Plaut A. G. IgA protease production as a characteristic distinguishing pathogenic from harmless neisseriaceae. N Engl J Med. 1978 Nov 2;299(18):973–976. doi: 10.1056/NEJM197811022991802. [DOI] [PubMed] [Google Scholar]
  16. Plaut A. G., Gilbert J. V., Artenstein M. S., Capra J. D. Neisseria gonorrhoeae and neisseria meningitidis: extracellular enzyme cleaves human immunoglobulin A. Science. 1975 Dec 12;190(4219):1103–1105. doi: 10.1126/science.810892. [DOI] [PubMed] [Google Scholar]
  17. Plaut A. G., Gilbert J. V., Heller I. Assay and properties of IgA protease of Streptococcus sanguis. Adv Exp Med Biol. 1978;107:489–495. doi: 10.1007/978-1-4684-3369-2_55. [DOI] [PubMed] [Google Scholar]
  18. Plaut A. G., Wistar R., Jr, Capra J. D. Differential susceptibility of human IgA immunoglobulins to streptococcal IgA protease. J Clin Invest. 1974 Dec;54(6):1295–1300. doi: 10.1172/JCI107875. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sakano H., Rogers J. H., Hüppi K., Brack C., Traunecker A., Maki R., Wall R., Tonegawa S. Domains and the hinge region of an immunoglobulin heavy chain are encoded in separate DNA segments. Nature. 1979 Feb 22;277(5698):627–633. doi: 10.1038/277627a0. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES