Abstract
Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS10GIL·NH2) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA10KGLPTLISWI20KNR·NH2) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (≤8μM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.
| Original language | English |
|---|---|
| Pages (from-to) | 496-500 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 306 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jun 27 2003 |
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Keywords
- Antimicrobial
- Antiviral
- Cytolytic
- Frog skin
- Hemolytic
- Melittin
- Temporin
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties. / Conlon, J. Michael; Sonnevend, Agnes; Patel, Mahendra; Camasamudram, Vijayayasarathy; Nowotny, Norbert; Zilahi, Erika; Iwamuro, Shawichi; Nielsen, Per F.; Pál, Tibor.
In: Biochemical and Biophysical Research Communications, Vol. 306, No. 2, 27.06.2003, p. 496-500.Research output: Contribution to journal › Article
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TY - JOUR
T1 - A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties
AU - Conlon, J. Michael
AU - Sonnevend, Agnes
AU - Patel, Mahendra
AU - Camasamudram, Vijayayasarathy
AU - Nowotny, Norbert
AU - Zilahi, Erika
AU - Iwamuro, Shawichi
AU - Nielsen, Per F.
AU - Pál, Tibor
PY - 2003/6/27
Y1 - 2003/6/27
N2 - Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS10GIL·NH2) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA10KGLPTLISWI20KNR·NH2) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (≤8μM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.
AB - Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS10GIL·NH2) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA10KGLPTLISWI20KNR·NH2) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (≤8μM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.
KW - Antimicrobial
KW - Antiviral
KW - Cytolytic
KW - Frog skin
KW - Hemolytic
KW - Melittin
KW - Temporin
UR - http://www.scopus.com/inward/record.url?scp=0038546578&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0038546578&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(03)00999-9
DO - 10.1016/S0006-291X(03)00999-9
M3 - Article
C2 - 12804591
AN - SCOPUS:0038546578
VL - 306
SP - 496
EP - 500
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -