Cargando…
Lipid Transfer Proteins (LTPs)—Structure, Diversity and Roles beyond Antimicrobial Activity
Lipid transfer proteins (LTPs) are among the most promising plant-exclusive antimicrobial peptides (AMPs). They figure among the most challenging AMPs from the point of view of their structural diversity, functions and biotechnological applications. This review presents a current picture of the LTP...
Autores principales: | , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8615156/ https://www.ncbi.nlm.nih.gov/pubmed/34827219 http://dx.doi.org/10.3390/antibiotics10111281 |
_version_ | 1784604036568186880 |
---|---|
author | Amador, Vinícius Costa dos Santos-Silva, Carlos André Vilela, Lívia Maria Batista Oliveira-Lima, Marx de Santana Rêgo, Mireli Roldan-Filho, Ricardo Salas de Oliveira-Silva, Roberta Lane Lemos, Ayug Bezerra de Oliveira, Wilson Dias Ferreira-Neto, José Ribamar Costa Crovella, Sérgio Benko-Iseppon, Ana Maria |
author_facet | Amador, Vinícius Costa dos Santos-Silva, Carlos André Vilela, Lívia Maria Batista Oliveira-Lima, Marx de Santana Rêgo, Mireli Roldan-Filho, Ricardo Salas de Oliveira-Silva, Roberta Lane Lemos, Ayug Bezerra de Oliveira, Wilson Dias Ferreira-Neto, José Ribamar Costa Crovella, Sérgio Benko-Iseppon, Ana Maria |
author_sort | Amador, Vinícius Costa |
collection | PubMed |
description | Lipid transfer proteins (LTPs) are among the most promising plant-exclusive antimicrobial peptides (AMPs). They figure among the most challenging AMPs from the point of view of their structural diversity, functions and biotechnological applications. This review presents a current picture of the LTP research, addressing not only their structural, evolutionary and further predicted functional aspects. Traditionally, LTPs have been identified by their direct isolation by biochemical techniques, whereas omics data and bioinformatics deserve special attention for their potential to bring new insights. In this context, new possible functions have been identified revealing that LTPs are actually multipurpose, with many additional predicted roles. Despite some challenges due to the toxicity and allergenicity of LTPs, a systematic review and search in patent databases, indicate promising perspectives for the biotechnological use of LTPs in human health and also plant defense. |
format | Online Article Text |
id | pubmed-8615156 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86151562021-11-26 Lipid Transfer Proteins (LTPs)—Structure, Diversity and Roles beyond Antimicrobial Activity Amador, Vinícius Costa dos Santos-Silva, Carlos André Vilela, Lívia Maria Batista Oliveira-Lima, Marx de Santana Rêgo, Mireli Roldan-Filho, Ricardo Salas de Oliveira-Silva, Roberta Lane Lemos, Ayug Bezerra de Oliveira, Wilson Dias Ferreira-Neto, José Ribamar Costa Crovella, Sérgio Benko-Iseppon, Ana Maria Antibiotics (Basel) Review Lipid transfer proteins (LTPs) are among the most promising plant-exclusive antimicrobial peptides (AMPs). They figure among the most challenging AMPs from the point of view of their structural diversity, functions and biotechnological applications. This review presents a current picture of the LTP research, addressing not only their structural, evolutionary and further predicted functional aspects. Traditionally, LTPs have been identified by their direct isolation by biochemical techniques, whereas omics data and bioinformatics deserve special attention for their potential to bring new insights. In this context, new possible functions have been identified revealing that LTPs are actually multipurpose, with many additional predicted roles. Despite some challenges due to the toxicity and allergenicity of LTPs, a systematic review and search in patent databases, indicate promising perspectives for the biotechnological use of LTPs in human health and also plant defense. MDPI 2021-10-21 /pmc/articles/PMC8615156/ /pubmed/34827219 http://dx.doi.org/10.3390/antibiotics10111281 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Amador, Vinícius Costa dos Santos-Silva, Carlos André Vilela, Lívia Maria Batista Oliveira-Lima, Marx de Santana Rêgo, Mireli Roldan-Filho, Ricardo Salas de Oliveira-Silva, Roberta Lane Lemos, Ayug Bezerra de Oliveira, Wilson Dias Ferreira-Neto, José Ribamar Costa Crovella, Sérgio Benko-Iseppon, Ana Maria Lipid Transfer Proteins (LTPs)—Structure, Diversity and Roles beyond Antimicrobial Activity |
title | Lipid Transfer Proteins (LTPs)—Structure, Diversity and Roles beyond Antimicrobial Activity |
title_full | Lipid Transfer Proteins (LTPs)—Structure, Diversity and Roles beyond Antimicrobial Activity |
title_fullStr | Lipid Transfer Proteins (LTPs)—Structure, Diversity and Roles beyond Antimicrobial Activity |
title_full_unstemmed | Lipid Transfer Proteins (LTPs)—Structure, Diversity and Roles beyond Antimicrobial Activity |
title_short | Lipid Transfer Proteins (LTPs)—Structure, Diversity and Roles beyond Antimicrobial Activity |
title_sort | lipid transfer proteins (ltps)—structure, diversity and roles beyond antimicrobial activity |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8615156/ https://www.ncbi.nlm.nih.gov/pubmed/34827219 http://dx.doi.org/10.3390/antibiotics10111281 |
work_keys_str_mv | AT amadorviniciuscosta lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT dossantossilvacarlosandre lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT vilelaliviamariabatista lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT oliveiralimamarx lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT desantanaregomireli lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT roldanfilhoricardosalas lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT deoliveirasilvarobertalane lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT lemosayugbezerra lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT deoliveirawilsondias lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT ferreiranetojoseribamarcosta lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT crovellasergio lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity AT benkoisepponanamaria lipidtransferproteinsltpsstructurediversityandrolesbeyondantimicrobialactivity |