Cloning and Expression of the IGA-Specific Endopeptidase
Genes from Neisseria meningitides

V. G. Khomenkov^a, T. N. Kazeeva^a, B. I. Shevelev^b, V. P. Bargrasser^c,
M. Yu. Skoblov^d, and A. B. Shevelev^a

^a Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 119071 Russia

^b City Center for Prophylaxis and Control of AIDS, Moscow, Russia

^c Institute of Experimental Cardiology, Russian Cardiology Research Center,
3-ya Cherepkovskaya ul. 15a, Moscow, 121552 Russia

^d Center of Medical Genetics, Russian Academy of Medical Sciences, Moscow, 115478 Russia

Received March 23, 2006

Abstract—IgA1-specific proteinases (Igase) are known as a pivotal pathogenicity factor in meningococcus
(Neisseria meningitides) and in some related bacteria. These enzymes belong to the trypsin-like clan of serine
proteases. They exhibit high substrate selectivity, being able to discriminate between IgAl and IgA2 and to dis-
tinguish the human IgAl from IgAl of nonprimate mammalian species [8]. According to recent data, in addition
to the conventional IgAl-processing enzymes, meningococci contain alternative enzymes. However, the sub-
strate specificity of the alternative Igase, its role in pathogenesis, and the ability to complement the functionality
of the conventional Igase remains obscure. In this study, we investigated the structure of the Igase genes and
their products in two highly virulent strains M9 and A208 of N. meningitides serogroup A. In particular, we
found both conventional and alternative Igase genes in each genome; the nucleotide sequences of these genes
were deposited in the NCBI Gene Bank under the accession numbers AY770504, AY558158, and AY558159.
The DNA sequence of the conventional Igase was almost entirely conserved in both strains, whereas the
recently discovered alternative Igase (formerly known as type 1 meningococcal adhesin) contained a hypervari-
able region approximately 900 bp long in the 5'-terminal part of the gene. The conventional genes from both
strains were expressed in E. coli in the form of inclusion bodies. The recombinant products were used for immu-
nization of rabbits. The antibodies obtained efficiently reacted with both recombinant and native antigens from
the N. meningitides culture medium.

DOI:10.3103/S0891416807010053

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