Immunoglobulin‐like domains of the cargo proteins are essential for protein stability during secretion by the type IX secretion system

Satô, Keiko; Kakuda, Shinji; Yukitake, Hideharu; Kondô, Yoshio; Shoji, Mikio; Takebe, Katsuki; Narita, Yuki; Naito, Mariko; Nakane, Daisuke; Abiko, Yoshimitsu; Hiratsuka, Koichi; Suzuki, Mamoru; Nakayama, Koji

doi:10.1111/mmi.14083

Cited by 18 publications

(17 citation statements)

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“…17 In particular, Kgp participates in the degradation of hemoglobin, which contains heme molecules, and accordingly, kgp mutants form unpigmented colonies on blood agar plates. [18][19][20] Using colony pigmentation, we discovered a Type IX secretion system (T9SS) that mediates the secretion of gingipains [21][22][23][24][25][26][27] and also determined the mechanism by which gingipains attach to the cell surface, which involves binding with anionic polysaccharide-containing LPS (A-LPS). [28][29][30][31][32][33] In P. gingivalis, the gingipains-A-LPS-pili triad interacts with one another and is a major contributor to the pathogenicity of the bacterium.…”

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confidence: 99%

Biogenesis of Type V pili

Shoji

Shibata

Sueyoshi

et al. 2020

Microbiology and Immunology

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Pili or fimbriae, which are filamentous structures present on the surface of bacteria, were purified from a periodontal pathogen, Porphyromonas gingivalis, in 1980s. The protein component of pili (stalk pilin), which is its major component, was named FimA; it has a molecular weight of approximately 41 kDa. Because the molecular weight of the pilin from P. gingivalis is twice that of pilins from other bacterial pili, the P. gingivalis Fim pili were suggested to be formed via a novel mechanism. In earlier studies, we reported that the FimA pilin is secreted on the cell surface as a lipoprotein precursor, and the subsequent N-terminal processing of the FimA precursor by arginine-specific proteases is necessary for Fim pili formation. The crystal structures of FimA and its related proteins were determined recently, which show that Fim pili are formed by a protease-mediated strand-exchange mechanism. The most recent study conducted by us, wherein we performed cryoelectron microscopy of the pilus structure, provided evidence in support of this mechanism. As the P. gingivalis Fim pili are formed through novel transport and assembly mechanisms, such pili are now designated as Type V pili. Surface lipoproteins, including the anchor pilin FimB of Fim pili that are present on the outer membrane, have been detected in certain Gram-negative bacteria. Here, we describe the assembly mechanisms of pili, including those of Type V and other pili, as well as the lipoprotein transport mechanisms. K E Y W O R D S bacterial components, lipoprotein, periodontal pathogen, pili 1 | INTRODUCTION Periodontal disease and dental caries are two leading causes of the loss of teeth worldwide. Periodontal disease is more commonly known to cause the loss of teeth than dental caries in people aged 40 years or above in Japan. 1 With age progression, the proportion of people with severe symptoms of periodontal disease increases as well and this tendency is noted approximately until individuals reach 80 years of age. 2,3 Chronic periodontitis is known to be caused by multiple bacteria that inhabit the periodontal pocket and the consequent immune responses. 4 Large-scale epidemiological studies have revealed the bacteria involved in the prevalence of periodontal disease. 5-7 Among periodontopathic bacteria, Porphyromonas gingivalis, Tannerella forsythia, and Treponema denticola are strongly associated with the onset and progression of chronic periodontitis and are

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confidence: 99%

Biogenesis of Type V pili

Shoji

Shibata

Sueyoshi

et al. 2020

Microbiology and Immunology

Self Cite

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“…Peptides derived from Titin ( 8990 ESDSG 8994 , 26941 EGNKDD 26946 , 6684 SSRLECKI 6691 , and 19103 VVHAGGVIRIIAYV 19116 ) and one peptide derived from striated muscle preferentially expressed protein kinase ( 2669 SCTVAVARVPGKLAPPEVPQ 2688 ) were located in Ig-like domains. The Ig-like domain was initially characterized as a structure composed of two sheets of antiparallel β strands [ 58 ]. Okano et al reported that the Ig-like domain contributed to the maintenance of the structure, activity, and stability of metagenome-derived glycoside hydrolase family 9 endoglucanase [ 59 ].…”

Section: Discussionmentioning

confidence: 99%

Peptidome analysis of umbilical cord mesenchymal stem cell (hUC-MSC) conditioned medium from preterm and term infants

Wang

Zhang

et al. 2020

Stem Cell Res Ther

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Background The therapeutic role of mesenchymal stem cells (MSCs) has been widely confirmed in several animal models of premature infant diseases. Micromolecule peptides have shown promise for the treatment of premature infant diseases. However, the potential role of peptides secreted from MSCs has not been studied. The purpose of this study is to help to broaden the knowledge of the hUC-MSC secretome at the peptide level through peptidomic profile analysis. Methods We used tandem mass tag (TMT) labeling technology followed by tandem mass spectrometry to compare the peptidomic profile of preterm and term umbilical cord MSC (hUC-MSC) conditioned medium (CM). Gene Ontology (GO) enrichment analysis and ingenuity pathway analysis (IPA) were conducted to explore the differentially expressed peptides by predicting the functions of their precursor proteins. To evaluate the effect of candidate peptides on human lung epithelial cells stimulated by hydrogen peroxide (H2O2), quantitative real-time PCR (qRT-PCR), western blot analysis, and enzyme-linked immunosorbent assay (ELISA) were, respectively, adopted to detect inflammatory cytokines (TNF-α, IL-1β, and IL-6) expression levels at the mRNA and protein levels. Results A total of 131 peptides derived from 106 precursor proteins were differentially expressed in the preterm hUC-MSC CM compared with the term group, comprising 37 upregulated peptides and 94 downregulated peptides. Bioinformatics analysis showed that these differentially expressed peptides may be associated with developmental disorders, inflammatory response, and organismal injury. We also found that peptides 7118TGAKIKLVGT7127 derived from MUC19 and 508AAAAGPANVH517 derived from SIX5 reduced the expression levels of TNF-α, IL-1β, and IL-6 in H2O2-treated human lung epithelial cells. Conclusions In summary, this study provides further secretomics information on hUC-MSCs and provides a series of peptides that might have antiinflammatory effects on pulmonary epithelial cells and contribute to the prevention and treatment of respiratory diseases in premature infants.

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“…Peptides derived from Titin ( 8990 ESDSG 8994 , 26941 EGNKDD 26946 , 6684 SSRLECKI 6691 and 19103 VVHAGGVIRIIAYV 19116 ) and one peptide derived from striated muscle preferentially expressed protein kinase ( 2669 SCTVAVARVPGKLAPPEVPQ 2688 ) were located in Ig-like domains. The Ig-like domain was initially characterized as a structure composed of two sheets of antiparallel β strands [59]. Okano et al reported that the Ig-like domain contributed to the maintenance of the structure, activity and stability of metagenome-derived glycoside hydrolase family 9 endoglucanase [60].…”

Section: Discussionmentioning

confidence: 99%

Peptidome Analysis of Umbilical Cord Mesenchymal Stem Cell (hUC-MSC) Conditioned Medium from Preterm and Term Infants

Wang

Zhang

et al. 2020

Preprint

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Background: The therapeutic role of mesenchymal stem cells (MSCs) has been widely confirmed in several animal models of premature infant diseases. Micromolecule peptides have shown promise for the treatment of premature infant diseases. However, the potential role of peptides secreted from MSCs has not been studied. The purpose of this study is to helps to broaden the knowledge of the hUC-MSC secretome at the peptide level through peptidomic profile analysis.Methods: We used tandem mass tag (TMT) labeling technology followed by tandem mass spectrometry to compare the peptidomic profile of preterm and term umbilical cord MSC (hUC-MSC) conditioned medium (CM). Gene Ontology (GO) enrichment analysis and Ingenuity Pathway Analysis (IPA) were conducted to explore the differentially expressed peptides by predicting the functions of their precursor proteins. To evaluate the effect of candidate peptides on human lung epithelial cells stimulated by hydrogen peroxide (H2O2), quantitative real-time PCR (qRT-PCR), western blot analysis and enzyme-linked immunosorbent assay (ELISA) were respectively adopted to detect inflammatory cytokines (TNF-α, IL-1β and IL-6) expression levels at the mRNA and protein levels,Results: A total of 131 peptides derived from 106 precursor proteins were differentially expressed in the preterm hUC-MSC CM compared with the term group, comprising 37 up-regulated peptides and 94 down-regulated peptides. Bioinformatics analysis showed that these differentially expressed peptides may be associated with developmental disorders, inflammatory response and organismal injury. We also found that peptides 7118TGAKIKLVGT7127 derived from MUC19 and 508AAAAGPANVH517 derived from SIX5 reduced the expression levels of TNF-α, IL-1β and IL-6 in H2O2-treated human lung epithelial cells.Conclusions: In summary, this study provides further secretomics information on hUC-MSCs and provides a series of peptides that might have antiinflammatory effects on pulmonary epithelial cells and contribute to the prevention and treatment of respiratory diseases in premature infants.

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Immunoglobulin‐like domains of the cargo proteins are essential for protein stability during secretion by the type IX secretion system

Cited by 18 publications

References 96 publications

Biogenesis of Type V pili

Biogenesis of Type V pili

Peptidome analysis of umbilical cord mesenchymal stem cell (hUC-MSC) conditioned medium from preterm and term infants

Peptidome Analysis of Umbilical Cord Mesenchymal Stem Cell (hUC-MSC) Conditioned Medium from Preterm and Term Infants

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