Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes

Detalhes bibliográficos
Autor(a) principal: Miranda, Luis Fernando B.
Data de Publicação: 2023
Outros Autores: Lima, Carolina V., Pagin, Rafaela, Costa, Raphael C., Pereira, Marta Maria A. [UNESP], de Avila, Erica D. [UNESP], Bertolini, Martinna, Retamal-Valdes, Belén, Shibli, Jamil A., Feres, Magda, Barão, Valentim A. R., Souza, João Gabriel S.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1021/acs.jproteome.2c00652
http://hdl.handle.net/11449/248374
Resumo: The use of saliva as a protein source prior to microbiological and biological assays requires previous processing. However, the effect of these processing methods on the proteomic profile of saliva has not been tested. Stimulated human saliva was collected from eight healthy volunteers. Non-processed saliva was compared with 0.22 μm filtered, 0.45 μm filtered, and pasteurized saliva, by liquid chromatography-mass spectrometry. Data are available via ProteomeXchange with identifier PXD039248. The effect of processed saliva on microbial adhesion was tested using bacterial and fungus species and in biological cell behavior using HaCaT immortalized human keratinocytes. Two hundred and seventy-eight proteins were identified in non-processed saliva, of which 54 proteins (≈19%) were exclusive. Saliva processing reduced identified proteins to 222 (≈80%) for the 0.22 μm group, 219 (≈79%) for the 0.45 μm group, and 201 (≈72%) for the pasteurized saliva, compared to non-processed saliva. The proteomic profile showed similar molecular functions and biological processes. The different saliva processing methods did not alter microbial adhesion (ANOVA, p > 0.05). Interestingly, pasteurized saliva reduced keratinocyte cell viability. Saliva processing methods tested reduced the proteomic profile diversity of saliva but maintained similar molecular functions and biological processes, not interfering with microbial adhesion and cell viability, except for pasteurization, which reduced cell viability.
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spelling Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processesmicrobiologyproteomicsalivasterilizationstudy modelThe use of saliva as a protein source prior to microbiological and biological assays requires previous processing. However, the effect of these processing methods on the proteomic profile of saliva has not been tested. Stimulated human saliva was collected from eight healthy volunteers. Non-processed saliva was compared with 0.22 μm filtered, 0.45 μm filtered, and pasteurized saliva, by liquid chromatography-mass spectrometry. Data are available via ProteomeXchange with identifier PXD039248. The effect of processed saliva on microbial adhesion was tested using bacterial and fungus species and in biological cell behavior using HaCaT immortalized human keratinocytes. Two hundred and seventy-eight proteins were identified in non-processed saliva, of which 54 proteins (≈19%) were exclusive. Saliva processing reduced identified proteins to 222 (≈80%) for the 0.22 μm group, 219 (≈79%) for the 0.45 μm group, and 201 (≈72%) for the pasteurized saliva, compared to non-processed saliva. The proteomic profile showed similar molecular functions and biological processes. The different saliva processing methods did not alter microbial adhesion (ANOVA, p > 0.05). Interestingly, pasteurized saliva reduced keratinocyte cell viability. Saliva processing methods tested reduced the proteomic profile diversity of saliva but maintained similar molecular functions and biological processes, not interfering with microbial adhesion and cell viability, except for pasteurization, which reduced cell viability.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Department of Prosthodontics and Periodontology Piracicaba Dental School University of Campinas (UNICAMP), Sa̅o PauloDepartment of Restorative Dentistry Federal University of Paraná (UFPR), ParanáDepartment of Periodontology Dental Research Division Guarulhos University (UnG), Sa̅o PauloDepartment of Dental Materials and Prosthodontics School of Dentistry at Araraquara São Paulo State University (UNESP), São PauloDepartment of Dental Materials and Prosthodontics School of Dentistry at Araçatuba São Paulo State University (UNESP), São PauloDepartment of Periodontics and Preventive Dentistry School of Dental Medicine University of PittsburghDental Science School (Faculdade de Ciências Odontológicas - FCO), Minas GeraisDepartment of Dental Materials and Prosthodontics School of Dentistry at Araraquara São Paulo State University (UNESP), São PauloDepartment of Dental Materials and Prosthodontics School of Dentistry at Araçatuba São Paulo State University (UNESP), São PauloUniversidade Estadual de Campinas (UNICAMP)Universidade Federal do Paraná (UFPR)Guarulhos University (UnG)Universidade Estadual Paulista (UNESP)University of PittsburghDental Science School (Faculdade de Ciências Odontológicas - FCO)Miranda, Luis Fernando B.Lima, Carolina V.Pagin, RafaelaCosta, Raphael C.Pereira, Marta Maria A. [UNESP]de Avila, Erica D. [UNESP]Bertolini, MartinnaRetamal-Valdes, BelénShibli, Jamil A.Feres, MagdaBarão, Valentim A. R.Souza, João Gabriel S.2023-07-29T13:42:19Z2023-07-29T13:42:19Z2023-03-03info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article857-870http://dx.doi.org/10.1021/acs.jproteome.2c00652Journal of Proteome Research, v. 22, n. 3, p. 857-870, 2023.1535-39071535-3893http://hdl.handle.net/11449/24837410.1021/acs.jproteome.2c006522-s2.0-85148299432Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Proteome Researchinfo:eu-repo/semantics/openAccess2023-07-29T13:42:20Zoai:repositorio.unesp.br:11449/248374Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-07-29T13:42:20Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes
title Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes
spellingShingle Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes
Miranda, Luis Fernando B.
microbiology
proteomic
saliva
sterilization
study model
title_short Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes
title_full Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes
title_fullStr Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes
title_full_unstemmed Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes
title_sort Effect of Processing Methods of Human Saliva on the Proteomic Profile and Protein-Mediated Biological Processes
author Miranda, Luis Fernando B.
author_facet Miranda, Luis Fernando B.
Lima, Carolina V.
Pagin, Rafaela
Costa, Raphael C.
Pereira, Marta Maria A. [UNESP]
de Avila, Erica D. [UNESP]
Bertolini, Martinna
Retamal-Valdes, Belén
Shibli, Jamil A.
Feres, Magda
Barão, Valentim A. R.
Souza, João Gabriel S.
author_role author
author2 Lima, Carolina V.
Pagin, Rafaela
Costa, Raphael C.
Pereira, Marta Maria A. [UNESP]
de Avila, Erica D. [UNESP]
Bertolini, Martinna
Retamal-Valdes, Belén
Shibli, Jamil A.
Feres, Magda
Barão, Valentim A. R.
Souza, João Gabriel S.
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual de Campinas (UNICAMP)
Universidade Federal do Paraná (UFPR)
Guarulhos University (UnG)
Universidade Estadual Paulista (UNESP)
University of Pittsburgh
Dental Science School (Faculdade de Ciências Odontológicas - FCO)
dc.contributor.author.fl_str_mv Miranda, Luis Fernando B.
Lima, Carolina V.
Pagin, Rafaela
Costa, Raphael C.
Pereira, Marta Maria A. [UNESP]
de Avila, Erica D. [UNESP]
Bertolini, Martinna
Retamal-Valdes, Belén
Shibli, Jamil A.
Feres, Magda
Barão, Valentim A. R.
Souza, João Gabriel S.
dc.subject.por.fl_str_mv microbiology
proteomic
saliva
sterilization
study model
topic microbiology
proteomic
saliva
sterilization
study model
description The use of saliva as a protein source prior to microbiological and biological assays requires previous processing. However, the effect of these processing methods on the proteomic profile of saliva has not been tested. Stimulated human saliva was collected from eight healthy volunteers. Non-processed saliva was compared with 0.22 μm filtered, 0.45 μm filtered, and pasteurized saliva, by liquid chromatography-mass spectrometry. Data are available via ProteomeXchange with identifier PXD039248. The effect of processed saliva on microbial adhesion was tested using bacterial and fungus species and in biological cell behavior using HaCaT immortalized human keratinocytes. Two hundred and seventy-eight proteins were identified in non-processed saliva, of which 54 proteins (≈19%) were exclusive. Saliva processing reduced identified proteins to 222 (≈80%) for the 0.22 μm group, 219 (≈79%) for the 0.45 μm group, and 201 (≈72%) for the pasteurized saliva, compared to non-processed saliva. The proteomic profile showed similar molecular functions and biological processes. The different saliva processing methods did not alter microbial adhesion (ANOVA, p > 0.05). Interestingly, pasteurized saliva reduced keratinocyte cell viability. Saliva processing methods tested reduced the proteomic profile diversity of saliva but maintained similar molecular functions and biological processes, not interfering with microbial adhesion and cell viability, except for pasteurization, which reduced cell viability.
publishDate 2023
dc.date.none.fl_str_mv 2023-07-29T13:42:19Z
2023-07-29T13:42:19Z
2023-03-03
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1021/acs.jproteome.2c00652
Journal of Proteome Research, v. 22, n. 3, p. 857-870, 2023.
1535-3907
1535-3893
http://hdl.handle.net/11449/248374
10.1021/acs.jproteome.2c00652
2-s2.0-85148299432
url http://dx.doi.org/10.1021/acs.jproteome.2c00652
http://hdl.handle.net/11449/248374
identifier_str_mv Journal of Proteome Research, v. 22, n. 3, p. 857-870, 2023.
1535-3907
1535-3893
10.1021/acs.jproteome.2c00652
2-s2.0-85148299432
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of Proteome Research
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 857-870
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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