IgA1 Protease

IgAl proteases have unique structures and functions, but little is known about it. It is independent in processing and maturation due to its ability to self-cleave specific hinge-like sequences linking that domain (Pohlner et al., 1987). IgAl protease has high selectivity for target binding within the hinge region of IgAl antibody. According to targeting binding, IgA 1 protease is divided into two types: IgA 1 protease type 1 cleaved proline, second Pro - Ser bond in sequence rich in serine and threonine, and IgA 1 protease type 2 cut Pro - Threo bond. Octapeptide (Bachovchin et al., 1990; Senior and Woff, 2005; Batten et al., 2003; Se

The protease immunoglobulin A1 (IgA1) protease of the IgA family forms a highly heterogeneous group of extracellular endopeptidases produced by numerous bacterial pathogens colonizing the mucosal surface of humans. These enzymes specifically cleave human IgA1 and participate in immune system monitoring of human mucosa. There are many reports on the cloning of the iga gene encoding IgAl protease from Neisseria gonorrhoeae. Nucleotide sequence analysis revealed that the enzyme was generated as a large precursor with three functional domains, an N-terminal leader peptide, a protease and a carboxy terminal "helper" domain. We also confirmed the overall structural similarity with the iga gene of Neisseria meningitidis.

Comparison of the deduced amino acid sequence of the iga gene of Haemophilus influenzae serotype b with the deduced amino acid sequence of a similar protease from Neisseria gonorrhoeae reveals several domains with high homology. For H. influenzae IgA 1 protease, an enzyme secretion mechanism similar to Neisseria gonorrhoeae IgA 1 protease was proposed. Limited diversity has been found in the IgA 1 protease genes of Haemophilus influenzae and serotype b strains, which is useful from the viewpoint of vaccine preparation.

HIV - 1 protease is an aspartyl protease (16) which acts as a dimer. As mentioned above, protease activity is required to cleave Gag and Gag-Pol polyprotein precursors during virion maturation. The three-dimensional structure of the protease dimer has been determined. (17, 18) Knowledge of this structure resulted in a class of drugs targeting inhibition of HIV protease function. These antiviral compounds have greatly improved the treatment of people infected with HIV. The pol gene encodes reverse transcriptase. Pol has RNA-dependent and DNA-dependent polymerase activity. During reverse transcription, the polymerase generates a double-stranded DNA copy of the single-stranded genomic RNA dimer present in the virion. RNase H removes the original RNA template from the first DNA strand, thereby synthesizing the complementary strand of DNA.