Cargando…

Facile Labeling of Sieve Element Phloem-Protein Bodies Using the Reciprocal Oligosaccharide Probe OGA(488)

Sieve elements of many angiosperms contain structural phloem proteins (P-proteins) that can interact to create large P-protein bodies. P-protein bodies can occlude sieve plates upon injury but the range of functional and physiological roles of P-proteins remains uncertain, in part because of challen...

Descripción completa

Detalles Bibliográficos
Autores principales: Azizpor, Pakeeza, Sullivan, Lucy, Lim, Aedric, Groover, Andrew
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8867008/
https://www.ncbi.nlm.nih.gov/pubmed/35222474
http://dx.doi.org/10.3389/fpls.2022.809923
_version_ 1784655961008373760
author Azizpor, Pakeeza
Sullivan, Lucy
Lim, Aedric
Groover, Andrew
author_facet Azizpor, Pakeeza
Sullivan, Lucy
Lim, Aedric
Groover, Andrew
author_sort Azizpor, Pakeeza
collection PubMed
description Sieve elements of many angiosperms contain structural phloem proteins (P-proteins) that can interact to create large P-protein bodies. P-protein bodies can occlude sieve plates upon injury but the range of functional and physiological roles of P-proteins remains uncertain, in part because of challenges in labeling and visualization methods. Here, we show that a reciprocal oligosaccharide probe, OGA(488), can be used in rapid and sensitive labeling of P-protein bodies in Arabidopsis, poplar, snap bean and cucumber in histological sections. OGA(488) labeling of knockouts of the two Arabidopsis P-protein-encoding genes, AtSEOR1 and AtSEOR2, indicated that labeling is specific to AtSEOR2. That protein bodies were labeled and visible in Atseor1 knockouts indicates that heterodimerization of AtSEOR1 and AtSEOR2 may not be necessary for P-protein body formation. Double labeling with a previously characterized stain for P-proteins, sulphorhodamine 101, confirmed P-protein labeling and also higher specificity of OGA(488) for P-proteins. OGA(488) is thus robust and easily used to label P-proteins in histological sections of multiple angiosperm species.
format Online
Article
Text
id pubmed-8867008
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-88670082022-02-25 Facile Labeling of Sieve Element Phloem-Protein Bodies Using the Reciprocal Oligosaccharide Probe OGA(488) Azizpor, Pakeeza Sullivan, Lucy Lim, Aedric Groover, Andrew Front Plant Sci Plant Science Sieve elements of many angiosperms contain structural phloem proteins (P-proteins) that can interact to create large P-protein bodies. P-protein bodies can occlude sieve plates upon injury but the range of functional and physiological roles of P-proteins remains uncertain, in part because of challenges in labeling and visualization methods. Here, we show that a reciprocal oligosaccharide probe, OGA(488), can be used in rapid and sensitive labeling of P-protein bodies in Arabidopsis, poplar, snap bean and cucumber in histological sections. OGA(488) labeling of knockouts of the two Arabidopsis P-protein-encoding genes, AtSEOR1 and AtSEOR2, indicated that labeling is specific to AtSEOR2. That protein bodies were labeled and visible in Atseor1 knockouts indicates that heterodimerization of AtSEOR1 and AtSEOR2 may not be necessary for P-protein body formation. Double labeling with a previously characterized stain for P-proteins, sulphorhodamine 101, confirmed P-protein labeling and also higher specificity of OGA(488) for P-proteins. OGA(488) is thus robust and easily used to label P-proteins in histological sections of multiple angiosperm species. Frontiers Media S.A. 2022-02-10 /pmc/articles/PMC8867008/ /pubmed/35222474 http://dx.doi.org/10.3389/fpls.2022.809923 Text en Copyright © 2022 Azizpor, Sullivan, Lim and Groover. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Azizpor, Pakeeza
Sullivan, Lucy
Lim, Aedric
Groover, Andrew
Facile Labeling of Sieve Element Phloem-Protein Bodies Using the Reciprocal Oligosaccharide Probe OGA(488)
title Facile Labeling of Sieve Element Phloem-Protein Bodies Using the Reciprocal Oligosaccharide Probe OGA(488)
title_full Facile Labeling of Sieve Element Phloem-Protein Bodies Using the Reciprocal Oligosaccharide Probe OGA(488)
title_fullStr Facile Labeling of Sieve Element Phloem-Protein Bodies Using the Reciprocal Oligosaccharide Probe OGA(488)
title_full_unstemmed Facile Labeling of Sieve Element Phloem-Protein Bodies Using the Reciprocal Oligosaccharide Probe OGA(488)
title_short Facile Labeling of Sieve Element Phloem-Protein Bodies Using the Reciprocal Oligosaccharide Probe OGA(488)
title_sort facile labeling of sieve element phloem-protein bodies using the reciprocal oligosaccharide probe oga(488)
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8867008/
https://www.ncbi.nlm.nih.gov/pubmed/35222474
http://dx.doi.org/10.3389/fpls.2022.809923
work_keys_str_mv AT azizporpakeeza facilelabelingofsieveelementphloemproteinbodiesusingthereciprocaloligosaccharideprobeoga488
AT sullivanlucy facilelabelingofsieveelementphloemproteinbodiesusingthereciprocaloligosaccharideprobeoga488
AT limaedric facilelabelingofsieveelementphloemproteinbodiesusingthereciprocaloligosaccharideprobeoga488
AT grooverandrew facilelabelingofsieveelementphloemproteinbodiesusingthereciprocaloligosaccharideprobeoga488