Serrulin: A Glycine-Rich Bioactive Peptide from the Hemolymph of the Yellow Tityus serrulatus Scorpion

Abstract

Antimicrobial peptides (AMPs) are small molecules, which have a potential use as antibiotic or pharmacological tools. In chelicerate organisms, such as scorpions, these molecules constitute an alternative defense system against microorganisms. The aim of this work was to identify AMPs in the hemolymph of the Tityus serrulatus scorpion. Fractions of plasma and hemocytes were subjected to high-performance liquid chromatography (HPLC) and then analyzed to determine their activity in inhibiting microbial growth. One of the fractions from the hemocytes presents antimicrobial activity against microorganisms, such as Gram-negative and Gram-positive bacteria, fungi, and yeast. These fractions were analyzed by mass spectrometry, and a fragment of 3564 Da. was identified. The peptide was called serrulin, because it is derived from the species T. serrulatus. A comparison of the amino acid sequence of serrulin with databases shows that it has a similarity to the glycine-rich peptides described in Cupienius salai and Acanthoscurria gomesiana (spiders). Furthermore, serrulin has no hemolytic activity against human erythrocytes. While the presence of AMPs in T. serrulatus venom has been described in other works, this is the first work to characterize the presence of these molecules in the hemolymph (hemocytes) of this species and show its potential use as an alternative to conventional antibiotics against different species of microorganisms.

A designed antimicrobial peptide with potential ability against methicillin resistant Staphylococcus aureus

“…According to the known AMPs, the hydrophobic tryptophan (Trp) residue prefers the interfacial region of lipid bilayers, and positively changed residues, like lysine (Lys) and arginine (Arg), facilitate the interaction of the AMPs with the anionic components of the bacterial membrane ( Jin et al, 2016 ). Furthermore, glycine (Gly) is frequently found in many antimicrobial peptides, which determines the antimicrobial activities ( Van Kan et al, 2001 ; De Jesus Oliveira et al, 2019 ).…”

Early Changes in Crayfish Hemocyte Proteins after Injection with a β-1,3-glucan, Compared to Saline Injected and Naive Animals

“…The available sequence shows similarities to Procambarin, a peptide identified from hemocytes of Procambarus clarkii [ 57 ]. Glycine-rich peptides described in other species, such as Scylla paramamosain , Acanthoscurria gomesiana , Armadillidium vulgare and Tityus serrulatus , generally exhibit broad and potent antimicrobial activity [ 58 , 59 , 60 , 61 ] The putative chitin-binding protein is another interesting find, as it could be a fungal infection-specific immune protein, since chitin is a common component of fungal cell walls. However, without further characterization, it is difficult to judge the specific functions of this protein.…”

A nematode-derived, mitochondrial stress signaling-regulated peptide exhibits broad antibacterial activity

“…We currently do not know the functional significance of this repeat sequence but interestingly, it is also found in a crustacean antimicrobial peptide that exhibits specific activity against Gram-positive bacteria ( Imjongjirak et al, 2011 ). Other glycine-rich antimicrobial peptides have also been discovered that exhibit activities against fungi and/or bacteria (both Gram-negative and Gram-positive) ( Bulet et al, 1991 ; de Jesus Oliveira et al, 2019 ; Lorenzini et al, 2003 ; Lu and Chen, 2010 ; Sousa et al, 2009 ; Sperstad et al, 2009 ; Verdon et al, 2016 ; Xie et al, 2020 ). While the caenacins were previously shown to possess anti-fungal properties, our study clearly demonstrates an antibacterial activity for CNC-4 against both Gram-negative and Gram-positive bacteria.…”