Pathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections
Prevalence of fungal diseases has increased globally in recent years, which often associated with increased immunocompromised patients, aging populations, and the novel Coronavirus pandemic. Furthermore, due to the limitation of available antifungal agents mortality and morbidity rates of invasion f...
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Frontiers Media S.A.
2021
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oai:doaj.org-article:17314e7c4f194f2e9fd0370242421bd92021-12-02T09:30:23ZPathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections2235-298810.3389/fcimb.2021.774340https://doaj.org/article/17314e7c4f194f2e9fd0370242421bd92021-12-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fcimb.2021.774340/fullhttps://doaj.org/toc/2235-2988Prevalence of fungal diseases has increased globally in recent years, which often associated with increased immunocompromised patients, aging populations, and the novel Coronavirus pandemic. Furthermore, due to the limitation of available antifungal agents mortality and morbidity rates of invasion fungal disease remain stubbornly high, and the emergence of multidrug-resistant fungi exacerbates the problem. Fungal pathogenicity and interactions between fungi and host have been the focus of many studies, as a result, lots of pathogenic mechanisms and fungal virulence factors have been identified. Mass spectrometry (MS)-based proteomics is a novel approach to better understand fungal pathogenicities and host–pathogen interactions at protein and protein posttranslational modification (PTM) levels. The approach has successfully elucidated interactions between pathogens and hosts by examining, for example, samples of fungal cells under different conditions, body fluids from infected patients, and exosomes. Many studies conclude that protein and PTM levels in both pathogens and hosts play important roles in progression of fungal diseases. This review summarizes mass spectrometry studies of protein and PTM levels from perspectives of both pathogens and hosts and provides an integrative conceptual outlook on fungal pathogenesis, antifungal agents development, and host–pathogen interactions.Yanjian LiHailong LiTianshu SunTianshu SunChen DingFrontiers Media S.A.articlefungal pathogensproteomemass spectrometryvirulence factorshost–pathogen interactionposttranslational modificationMicrobiologyQR1-502ENFrontiers in Cellular and Infection Microbiology, Vol 11 (2021) |
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topic |
fungal pathogens proteome mass spectrometry virulence factors host–pathogen interaction posttranslational modification Microbiology QR1-502 |
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fungal pathogens proteome mass spectrometry virulence factors host–pathogen interaction posttranslational modification Microbiology QR1-502 Yanjian Li Hailong Li Tianshu Sun Tianshu Sun Chen Ding Pathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections |
description |
Prevalence of fungal diseases has increased globally in recent years, which often associated with increased immunocompromised patients, aging populations, and the novel Coronavirus pandemic. Furthermore, due to the limitation of available antifungal agents mortality and morbidity rates of invasion fungal disease remain stubbornly high, and the emergence of multidrug-resistant fungi exacerbates the problem. Fungal pathogenicity and interactions between fungi and host have been the focus of many studies, as a result, lots of pathogenic mechanisms and fungal virulence factors have been identified. Mass spectrometry (MS)-based proteomics is a novel approach to better understand fungal pathogenicities and host–pathogen interactions at protein and protein posttranslational modification (PTM) levels. The approach has successfully elucidated interactions between pathogens and hosts by examining, for example, samples of fungal cells under different conditions, body fluids from infected patients, and exosomes. Many studies conclude that protein and PTM levels in both pathogens and hosts play important roles in progression of fungal diseases. This review summarizes mass spectrometry studies of protein and PTM levels from perspectives of both pathogens and hosts and provides an integrative conceptual outlook on fungal pathogenesis, antifungal agents development, and host–pathogen interactions. |
format |
article |
author |
Yanjian Li Hailong Li Tianshu Sun Tianshu Sun Chen Ding |
author_facet |
Yanjian Li Hailong Li Tianshu Sun Tianshu Sun Chen Ding |
author_sort |
Yanjian Li |
title |
Pathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections |
title_short |
Pathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections |
title_full |
Pathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections |
title_fullStr |
Pathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections |
title_full_unstemmed |
Pathogen-Host Interaction Repertoire at Proteome and Posttranslational Modification Levels During Fungal Infections |
title_sort |
pathogen-host interaction repertoire at proteome and posttranslational modification levels during fungal infections |
publisher |
Frontiers Media S.A. |
publishDate |
2021 |
url |
https://doaj.org/article/17314e7c4f194f2e9fd0370242421bd9 |
work_keys_str_mv |
AT yanjianli pathogenhostinteractionrepertoireatproteomeandposttranslationalmodificationlevelsduringfungalinfections AT hailongli pathogenhostinteractionrepertoireatproteomeandposttranslationalmodificationlevelsduringfungalinfections AT tianshusun pathogenhostinteractionrepertoireatproteomeandposttranslationalmodificationlevelsduringfungalinfections AT tianshusun pathogenhostinteractionrepertoireatproteomeandposttranslationalmodificationlevelsduringfungalinfections AT chending pathogenhostinteractionrepertoireatproteomeandposttranslationalmodificationlevelsduringfungalinfections |
_version_ |
1718398051162259456 |