Page 26 - O. Microbiology

[O. Microbiology-21]

Lycotoxin-Pa2a, A novel antibacterial and antifungal peptide

derived from the venom of the spider Pardosa astrigera

Yunkyung Kim¹, Min Kyoung Shin¹˙#, In-Wook Hwang¹, Seung-Tae Kim², Jung-Suk Sung¹˙*

¹Department of Life Science, Dongguk University-Seoul, Goyang 10326, Republic of Korea, ²Life and Environment

Research Institute, Konkuk University, Seoul 05029, Republic of Korea

Venom of spiders consists of various bioactive peptides including antimicrobial peptides (AMPs). RNA sequencing
and transcriptome construction was performed to find functional AMPs from the venom gland of the spider Pardosa

astrigera. Following homology search against known toxin peptides, structural characterization of confirmed

sequences was conducted. A novel toxin-like peptide with a cationic, α-helical conformation in the C-terminus was
selected and named Lycotoxin-Pa2a. The peptide inhibited the growth of gram-positive and gram-negative bacteria
as well as methicillin-resistant Staphylococcus aureus. The antibacterial mechanism of Lycotoxin-Pa2a was evaluated

by membrane permeability assay using NPN and DiSC3(5). Also, the peptide showed antifungal activity against
Fusarium oxysporum and Candida albicans. In this study, the transcriptome and in silico analysis identified a novel

peptide Lycotoxin-Pa2a, which exhibited antimicrobial activity. These results suggest the potential of peptides
derived from spider venom for the development of new anti-infective agents. [This work was supported by a grant

from the National Institute of Biological Resources (NIBR), funded by the Ministry of Environment (MOE) of the
Republic of Korea (NIBR202009201)]