Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry

We report the application of a hybrid element and molecular MS configuration for the parallel absolute quantification of uHPLC-separated intact sulfur-containing venom proteins, via ICP triple quadrupole MS and 32S/34S isotope dilution analysis, and identification by ESI-QToF-MS of the toxins of the...

Descripción completa

Detalles Bibliográficos
Autores: Calderón Celis, Francisco, Cid-Barrio, Laura, Ruiz Encinar, Jorge, Sanz-Medel, Alfredo, Calvete, Juan J.
Tipo de recurso: artículo
Fecha de publicación:2017
País:España
Institución:Universidad de Cantabria (UC)
Repositorio:UCrea Repositorio Abierto de la Universidad de Cantabria
Idioma:inglés
OAI Identifier:oai:repositorio.unican.es:10902/39487
Acceso en línea:https://hdl.handle.net/10902/39487
Access Level:acceso abierto
Palabra clave:Hybrid mas spectrometry configuration
Elemental mass spectrometry
ICPQQQ MS
Absolute protein quantification
Isotope dilution
Snake venomics
id ES_862dc3ee35726cbbb231a23601a86e39
oai_identifier_str oai:repositorio.unican.es:10902/39487
network_acronym_str ES
network_name_str España
repository_id_str
spelling Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometryCalderón Celis, FranciscoCid-Barrio, LauraRuiz Encinar, JorgeSanz-Medel, AlfredoCalvete, Juan J.Hybrid mas spectrometry configurationElemental mass spectrometryICPQQQ MSAbsolute protein quantificationIsotope dilutionSnake venomicsWe report the application of a hybrid element and molecular MS configuration for the parallel absolute quantification of uHPLC-separated intact sulfur-containing venom proteins, via ICP triple quadrupole MS and 32S/34S isotope dilution analysis, and identification by ESI-QToF-MS of the toxins of the medically important African black-necked spitting cobra, Naja nigricollis (Tanzania); New Guinea small-eyed snake, Micropechis ikaheka; and Papuan black snake, Pseudechis papuanus. The main advantage of this approach is that only one generic sulfur-containing standard is required to quantify each and all intact Cys- and/or Met-containing toxins of the venom proteome. The results of absolute quantification are in reasonably good agreement with previously reported relative quantification of the most abundant protein families. However, both datasets depart in the quantification of the minor ones, showing a tendency for this set of proteins to be underestimated in standard peptide-centric venomics approaches. The molecular identity, specific toxic activity, and concentration in the venom, are the pillars on which the toxicovenomics-aimed discovery of the most medically-relevant venom toxins, e.g. those that need to be neutralized by an effective therapeutic antivenom, should be based. The pioneering venom proteome-wide absolute quantification shown in this paper represents thus a significant advance towards this goal. The potential of ICP triple quadrupole MS in proteomics in general, and venomics in particular, is critically discussed.Authors wish to thank Agilent and Agilent Foundation for the generous technical and financial support, and Quality Assistance for financial support. This study was supported by Grants BES-2014-068032 (F.C.C.), CTQ2013-49032-C2-1-R (A.S.M.), CTQ2016-79412-P (J.R.E.), and BFU2013-42833-P (J.J.C) from the Ministerio de Economía y Competitividad, Madrid, Spain, and Grant FPU15/04989 (L.C.B.) from the Ministerio de Educación, Madrid, Spain. The assistance during ESI-QToF analyses of Dr. Sergio Cueto Diaz, from Scientific Services of University of Oviedo, is also gratefully acknowledged.Elsevier BVUniversidad de Cantabria20172017-01-01journal articlehttp://purl.org/coar/resource_type/c_6501NAhttp://purl.org/coar/version/c_be7fb7dd8ff6fe43info:eu-repo/semantics/articlehttps://hdl.handle.net/10902/39487Journal of Proteomics, 2017, 164, 33-42reponame:UCrea Repositorio Abierto de la Universidad de Cantabriainstname:Universidad de Cantabria (UC)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:repositorio.unican.es:10902/394872026-06-02T12:39:31Z
dc.title.none.fl_str_mv Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry
title Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry
spellingShingle Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry
Calderón Celis, Francisco
Hybrid mas spectrometry configuration
Elemental mass spectrometry
ICPQQQ MS
Absolute protein quantification
Isotope dilution
Snake venomics
title_short Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry
title_full Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry
title_fullStr Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry
title_full_unstemmed Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry
title_sort Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry
dc.creator.none.fl_str_mv Calderón Celis, Francisco
Cid-Barrio, Laura
Ruiz Encinar, Jorge
Sanz-Medel, Alfredo
Calvete, Juan J.
author Calderón Celis, Francisco
author_facet Calderón Celis, Francisco
Cid-Barrio, Laura
Ruiz Encinar, Jorge
Sanz-Medel, Alfredo
Calvete, Juan J.
author_role author
author2 Cid-Barrio, Laura
Ruiz Encinar, Jorge
Sanz-Medel, Alfredo
Calvete, Juan J.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidad de Cantabria
dc.subject.none.fl_str_mv Hybrid mas spectrometry configuration
Elemental mass spectrometry
ICPQQQ MS
Absolute protein quantification
Isotope dilution
Snake venomics
topic Hybrid mas spectrometry configuration
Elemental mass spectrometry
ICPQQQ MS
Absolute protein quantification
Isotope dilution
Snake venomics
description We report the application of a hybrid element and molecular MS configuration for the parallel absolute quantification of uHPLC-separated intact sulfur-containing venom proteins, via ICP triple quadrupole MS and 32S/34S isotope dilution analysis, and identification by ESI-QToF-MS of the toxins of the medically important African black-necked spitting cobra, Naja nigricollis (Tanzania); New Guinea small-eyed snake, Micropechis ikaheka; and Papuan black snake, Pseudechis papuanus. The main advantage of this approach is that only one generic sulfur-containing standard is required to quantify each and all intact Cys- and/or Met-containing toxins of the venom proteome. The results of absolute quantification are in reasonably good agreement with previously reported relative quantification of the most abundant protein families. However, both datasets depart in the quantification of the minor ones, showing a tendency for this set of proteins to be underestimated in standard peptide-centric venomics approaches. The molecular identity, specific toxic activity, and concentration in the venom, are the pillars on which the toxicovenomics-aimed discovery of the most medically-relevant venom toxins, e.g. those that need to be neutralized by an effective therapeutic antivenom, should be based. The pioneering venom proteome-wide absolute quantification shown in this paper represents thus a significant advance towards this goal. The potential of ICP triple quadrupole MS in proteomics in general, and venomics in particular, is critically discussed.
publishDate 2017
dc.date.none.fl_str_mv 2017
2017-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
NA
http://purl.org/coar/version/c_be7fb7dd8ff6fe43
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/10902/39487
url https://hdl.handle.net/10902/39487
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier BV
publisher.none.fl_str_mv Elsevier BV
dc.source.none.fl_str_mv Journal of Proteomics, 2017, 164, 33-42
reponame:UCrea Repositorio Abierto de la Universidad de Cantabria
instname:Universidad de Cantabria (UC)
instname_str Universidad de Cantabria (UC)
reponame_str UCrea Repositorio Abierto de la Universidad de Cantabria
collection UCrea Repositorio Abierto de la Universidad de Cantabria
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869412354818572288
score 15,811543

Similares en LA Referencia