Molecular Characterization and Phylogenetic Analysis of Novel Isoform of Anti-lipopolysaccharide Factor from the Mantis Shrimp, Miyakea Nepa

Overview

Journal Probiotics Antimicrob Proteins

Publisher Springer

Specialties Infectious Diseases
Microbiology
Nutritional Sciences
Pharmacology

Date 2015 Jul 19

PMID 26187684

Citations 4

Authors

K S Sruthy

E R Chaithanya

Naveen Sathyan

Aishwarya Nair

Swapna P Antony

I S Bright Singh

Rosamma Philip

Affiliations

Soon will be listed here.

Abstract

Anti-lipopolysaccharide factor (ALF) is a cationic anti-microbial peptide representing humoral defence system exhibiting a diverse spectrum of activity against microbial pathogens, including gram-negative and gram-positive bacteria, fungi, parasites and viruses. In this study, we identified and characterized a novel ALF homologue (MnALF) encoding cDNA sequence from the haemocytes of stomatopod mantis shrimp Miyakea nepa. The deduced peptide of MnALF encoded for a 123-amino acid peptide with a 25-residue signal peptide containing selenocysteine followed by a highly cationic mature peptide comprised of a putative LPS-binding domain flanked by two cysteine residues. BLAST analysis of MnALF showed that it exhibits identity to crustacean and limulid ALFs. The mature peptide of MnALF has a net charge of +7 and predicted molecular weight of 10.998 kDa with a theoretical isoelectric point (pI) of 9.93. Spatial structure of MnALF comprises three α-helices packed against a four-stranded β-sheet of which two were linked by a disulphide bond to form an amphipathic loop similar to the structure of Penaeus monodon, ALF-Pm3. All these features suggest that MnALF could play an imperative role in the innate defence mechanism of M. nepa. To our knowledge, this study accounts for the first report of an anti-microbial peptide from the order stomatopoda.

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