A fibrinolytic metalloprotease gene from Bacillus subtilis has been cloned in Escheridria coli XL1-Blue and the bacterial expressed enzyme was purified. The nucleotide sequence of the cloned fibrinolytic enzyme gene revealed a single open reading frame of 1023 bp coding for 341 amino acids (M r 37708.21 Da). N-terminal amino acid sequencing of the fibrinolytic enzyme excreted from E. coli host cells revealed that the mature fibrinolytic enzyme consists of 288 amino acids (M r 31391.1 Da). The deduced amino acid sequence showed significant homology with Erwina carotovora neutral metalloprotease and Serratia marcescens minor metalloprotease by 65 and 58% amino acid sequence identity, respectively. The protein showed significant alignments with the conserved domain of catalytic activity and the a-helix domain in Bacillus anthracis thermolysis metalloprotease. The biochemical properties of the purified enzyme suggested that the enzyme is a fibrinolytic metalloprotease, which has optimal activity at pH 7.0 and 50°C.

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Innate immunity is the first line of host defense consisting of various molecules against infectious challenges. Mannose-binding lectin (MBL) belongs to the collectin protein family which takes part of innate immunity and is able to recognize specific carbohydrates on the surface of a variety of infectious agents acting as a pattern recognition molecule. In this way, MBL differentiates self from non-self and interacts with other molecules of the immune system. MBL genotype shows various MBL2 polymorphisms which are responsible for MBL deficiency in a substantial portion of the entire human population and for susceptibility to infectious disease. Therefore, it has been highlighted in the relationship between genetic variants and clinical significance. Here we focus on presenting anoverview of our understanding of MBL structure and functions.

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