Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)

Milena Mechkarska; G Barran; J Kolodziejek; L Coquet; J Leprince; T Jouenne; N Nowotny; John Michael Conlon

doi:10.1016/j.cbd.2023.101069

Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)

Milena Mechkarska, G Barran, J Kolodziejek, L Coquet, J Leprince, T Jouenne, N Nowotny, John Michael Conlon

School of Biomedical Sciences

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Abstract

Skin secretions of certain frog species represent a source of host-defense peptides (HDPs) with therapeutic potential and their primary structures provide insight into taxonomic and phylogenetic relationships. Peptidomic analysis was used to characterize the HDPs in norepinephrine-stimulated skin secretions from the Amazon River frog Lithobates palmipes (Ranidae) collected in Trinidad. A total of ten peptides were purified and identified on the basis of amino acid similarity as belonging to the ranatuerin-2 family (ranatuerin-2PMa, -2PMb, -2PMc, and-2PMd), the brevinin-1 family (brevinin-1PMa, -1PMb, -1PMc and des(8–14)brevinin-1PMa) and the temporin family (temporin-PMa in C-terminally amidated and non-amidated forms). Deletion of the sequence VAAKVLP from brevinin-1PMa (FLPLIAGVAAKVLPKIFCAISKKC) in des[(8–14)brevinin-1PMa resulted in a 10-fold decrease in potency against Staphylococcus aureus (MIC = 31 μM compared with 3 μM) and a > 50-fold decrease in hemolytic activity but potency against Echerichia coli was maintained (MIC = 62.5 μM compared with 50 μM). Temporin-PMa (FLPFLGKLLSGIF.NH ₂) inhibited growth of S. aureus (MIC = 16 μM) but the non-amidated form of the peptide lacked antimicrobial activity. Cladistic analysis based upon the primary structures of ranaturerin-2 peptides supports the division of New World frogs of the family Ranidae into the genera Lithobates and Rana. A sister-group relationship between L. palmipes and Warszewitsch's frog Lithobates warszewitschii is indicated within a clade that includes the Tarahumara frog Lithobates tarahumarae. The study has provided further evidence that peptidomic analysis of HDPs in frog skin secretions is a valuable approach to elucidation of the evolutionary history of species within a particular genus.

Original language	English
Article number	101069
Pages (from-to)	101069
Journal	Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics
Volume	46
Early online date	24 Feb 2023
DOIs	https://doi.org/10.1016/j.cbd.2023.101069
Publication status	Published (in print/issue) - 30 Jun 2023

Bibliographical note

Funding Information:
Experimental work was supported by a Campus Research & Publication grant (CRP.5.OCT18.66) and a travel grant (CRP.5.OCT19.94 awarded to GB from the School for Graduate Studies and Research, The University of the West Indies, St. Augustine Campus. A Study and Travel grant and Institutional Visit Allowance were awarded to MM. The authors thank Rainer Deo and Hukaymah Ali from West Indian Herping (Trinidad and Tobago) for providing expert advice and assistance during the field trip to collect frogs.

Publisher Copyright:
© 2023 The Author(s)

Keywords

Host-defense peptide
Antimicorbial
Frog skin
Brevinin-1
Ranatuerin-2
Temporin
Antimicrobial

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.cbd.2023.101069

Lithobates palmipesFinal published version, 2.4 MBLicence: CC BY

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Mechkarska, M., Barran, G., Kolodziejek, J., Coquet, L., Leprince, J., Jouenne, T., Nowotny, N., & Conlon, J. M. (2023). Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae). Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics, 46, 101069. Article 101069. https://doi.org/10.1016/j.cbd.2023.101069

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title = "Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)",

abstract = "Skin secretions of certain frog species represent a source of host-defense peptides (HDPs) with therapeutic potential and their primary structures provide insight into taxonomic and phylogenetic relationships. Peptidomic analysis was used to characterize the HDPs in norepinephrine-stimulated skin secretions from the Amazon River frog Lithobates palmipes (Ranidae) collected in Trinidad. A total of ten peptides were purified and identified on the basis of amino acid similarity as belonging to the ranatuerin-2 family (ranatuerin-2PMa, -2PMb, -2PMc, and-2PMd), the brevinin-1 family (brevinin-1PMa, -1PMb, -1PMc and des(8–14)brevinin-1PMa) and the temporin family (temporin-PMa in C-terminally amidated and non-amidated forms). Deletion of the sequence VAAKVLP from brevinin-1PMa (FLPLIAGVAAKVLPKIFCAISKKC) in des[(8–14)brevinin-1PMa resulted in a 10-fold decrease in potency against Staphylococcus aureus (MIC = 31 μM compared with 3 μM) and a > 50-fold decrease in hemolytic activity but potency against Echerichia coli was maintained (MIC = 62.5 μM compared with 50 μM). Temporin-PMa (FLPFLGKLLSGIF.NH 2) inhibited growth of S. aureus (MIC = 16 μM) but the non-amidated form of the peptide lacked antimicrobial activity. Cladistic analysis based upon the primary structures of ranaturerin-2 peptides supports the division of New World frogs of the family Ranidae into the genera Lithobates and Rana. A sister-group relationship between L. palmipes and Warszewitsch's frog Lithobates warszewitschii is indicated within a clade that includes the Tarahumara frog Lithobates tarahumarae. The study has provided further evidence that peptidomic analysis of HDPs in frog skin secretions is a valuable approach to elucidation of the evolutionary history of species within a particular genus.",

keywords = "Host-defense peptide, Antimicorbial, Frog skin, Brevinin-1, Ranatuerin-2, Temporin, Antimicrobial",

author = "Milena Mechkarska and G Barran and J Kolodziejek and L Coquet and J Leprince and T Jouenne and N Nowotny and Conlon, {John Michael}",

note = "Funding Information: Experimental work was supported by a Campus Research & Publication grant (CRP.5.OCT18.66) and a travel grant (CRP.5.OCT19.94 awarded to GB from the School for Graduate Studies and Research, The University of the West Indies, St. Augustine Campus. A Study and Travel grant and Institutional Visit Allowance were awarded to MM. The authors thank Rainer Deo and Hukaymah Ali from West Indian Herping (Trinidad and Tobago) for providing expert advice and assistance during the field trip to collect frogs. Publisher Copyright: {\textcopyright} 2023 The Author(s)",

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doi = "10.1016/j.cbd.2023.101069",

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Mechkarska, M, Barran, G, Kolodziejek, J, Coquet, L, Leprince, J, Jouenne, T, Nowotny, N & Conlon, JM 2023, 'Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)', Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics, vol. 46, 101069, pp. 101069. https://doi.org/10.1016/j.cbd.2023.101069

TY - JOUR

T1 - Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)

AU - Mechkarska, Milena

AU - Barran, G

AU - Kolodziejek, J

AU - Coquet, L

AU - Leprince, J

AU - Jouenne, T

AU - Nowotny, N

AU - Conlon, John Michael

N1 - Funding Information: Experimental work was supported by a Campus Research & Publication grant (CRP.5.OCT18.66) and a travel grant (CRP.5.OCT19.94 awarded to GB from the School for Graduate Studies and Research, The University of the West Indies, St. Augustine Campus. A Study and Travel grant and Institutional Visit Allowance were awarded to MM. The authors thank Rainer Deo and Hukaymah Ali from West Indian Herping (Trinidad and Tobago) for providing expert advice and assistance during the field trip to collect frogs. Publisher Copyright: © 2023 The Author(s)

PY - 2023/6/30

Y1 - 2023/6/30

N2 - Skin secretions of certain frog species represent a source of host-defense peptides (HDPs) with therapeutic potential and their primary structures provide insight into taxonomic and phylogenetic relationships. Peptidomic analysis was used to characterize the HDPs in norepinephrine-stimulated skin secretions from the Amazon River frog Lithobates palmipes (Ranidae) collected in Trinidad. A total of ten peptides were purified and identified on the basis of amino acid similarity as belonging to the ranatuerin-2 family (ranatuerin-2PMa, -2PMb, -2PMc, and-2PMd), the brevinin-1 family (brevinin-1PMa, -1PMb, -1PMc and des(8–14)brevinin-1PMa) and the temporin family (temporin-PMa in C-terminally amidated and non-amidated forms). Deletion of the sequence VAAKVLP from brevinin-1PMa (FLPLIAGVAAKVLPKIFCAISKKC) in des[(8–14)brevinin-1PMa resulted in a 10-fold decrease in potency against Staphylococcus aureus (MIC = 31 μM compared with 3 μM) and a > 50-fold decrease in hemolytic activity but potency against Echerichia coli was maintained (MIC = 62.5 μM compared with 50 μM). Temporin-PMa (FLPFLGKLLSGIF.NH 2) inhibited growth of S. aureus (MIC = 16 μM) but the non-amidated form of the peptide lacked antimicrobial activity. Cladistic analysis based upon the primary structures of ranaturerin-2 peptides supports the division of New World frogs of the family Ranidae into the genera Lithobates and Rana. A sister-group relationship between L. palmipes and Warszewitsch's frog Lithobates warszewitschii is indicated within a clade that includes the Tarahumara frog Lithobates tarahumarae. The study has provided further evidence that peptidomic analysis of HDPs in frog skin secretions is a valuable approach to elucidation of the evolutionary history of species within a particular genus.

AB - Skin secretions of certain frog species represent a source of host-defense peptides (HDPs) with therapeutic potential and their primary structures provide insight into taxonomic and phylogenetic relationships. Peptidomic analysis was used to characterize the HDPs in norepinephrine-stimulated skin secretions from the Amazon River frog Lithobates palmipes (Ranidae) collected in Trinidad. A total of ten peptides were purified and identified on the basis of amino acid similarity as belonging to the ranatuerin-2 family (ranatuerin-2PMa, -2PMb, -2PMc, and-2PMd), the brevinin-1 family (brevinin-1PMa, -1PMb, -1PMc and des(8–14)brevinin-1PMa) and the temporin family (temporin-PMa in C-terminally amidated and non-amidated forms). Deletion of the sequence VAAKVLP from brevinin-1PMa (FLPLIAGVAAKVLPKIFCAISKKC) in des[(8–14)brevinin-1PMa resulted in a 10-fold decrease in potency against Staphylococcus aureus (MIC = 31 μM compared with 3 μM) and a > 50-fold decrease in hemolytic activity but potency against Echerichia coli was maintained (MIC = 62.5 μM compared with 50 μM). Temporin-PMa (FLPFLGKLLSGIF.NH 2) inhibited growth of S. aureus (MIC = 16 μM) but the non-amidated form of the peptide lacked antimicrobial activity. Cladistic analysis based upon the primary structures of ranaturerin-2 peptides supports the division of New World frogs of the family Ranidae into the genera Lithobates and Rana. A sister-group relationship between L. palmipes and Warszewitsch's frog Lithobates warszewitschii is indicated within a clade that includes the Tarahumara frog Lithobates tarahumarae. The study has provided further evidence that peptidomic analysis of HDPs in frog skin secretions is a valuable approach to elucidation of the evolutionary history of species within a particular genus.

KW - Host-defense peptide

KW - Antimicorbial

KW - Frog skin

KW - Brevinin-1

KW - Ranatuerin-2

KW - Temporin

KW - Antimicrobial

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U2 - 10.1016/j.cbd.2023.101069

DO - 10.1016/j.cbd.2023.101069

M3 - Article

C2 - 36868141

SN - 1744-117X

VL - 46

SP - 101069

JO - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics

JF - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics

M1 - 101069

ER -

Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)

Abstract

Bibliographical note

Keywords

UN SDGs

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