Cell Proteins Obtained by Peptic Shaving of Two Phenotypically Different Strains of As a Source of Anti-Inflammatory Peptides

Overview

Journal Nutrients

Date 2022 Nov 26

PMID 36432464

Authors

Rania Allouche

Magali Genay

Annie Dary-Mourot

Zeeshan Hafeez

Laurent Miclo

Affiliations

Soon will be listed here.

Abstract

, a food grade bacterium, is extensively used in the manufacture of fermented products such as yogurt and cheeses. It has been shown that strains exhibited varying anti-inflammatory activities in vitro. Our previous study displayed that this activity could be partially due to peptide(s) generated by trypsin hydrolysis of the surface proteins of LMD-9. Surface protease PrtS could be the source of these peptides during gastrointestinal digestion. Therefore, peptide hydrolysates were obtained by shaving two phenotypically distinct strains of (LMD-9 PrtS and CNRZ-21N PrtS) with pepsin, a gastric protease, followed or not by trypsinolysis. The peptide hydrolysates of both strains exhibited anti-inflammatory action through the modulation of pro-inflammatory mediators in LPS-stimulated THP-1 macrophages (COX-2, Pro-IL-1β, IL-1β, and IL-8) and LPS-stimulated HT-29 cells (IL-8). Therefore, peptides released from either PrtS or PrtS strains in the gastrointestinal tract during digestion of a product containing this bacterium may display anti-inflammatory effects and reduce the risk of inflammation-related chronic diseases.

Citing Articles

: A Source of Postbiotics Displaying Anti-Inflammatory Effects in THP 1 Macrophages.

Allouche R, Hafeez Z, Dary-Mourot A, Genay M, Miclo L Molecules. 2024; 29(7).

PMID: 38611831 PMC: 11013757. DOI: 10.3390/molecules29071552.

References

Hols P, Hancy F, Fontaine L, Grossiord B, Prozzi D, Leblond-Bourget N . New insights in the molecular biology and physiology of Streptococcus thermophilus revealed by comparative genomics. FEMS Microbiol Rev. 2005; 29(3):435-63. DOI: 10.1016/j.femsre.2005.04.008. View

Boulay M, Metton C, Mezange C, Oliveira Correia L, Meylheuc T, Monnet V . Three Distinct Proteases Are Responsible for Overall Cell Surface Proteolysis in Streptococcus thermophilus. Appl Environ Microbiol. 2021; 87(23):e0129221. PMC: 8580001. DOI: 10.1128/AEM.01292-21. View

Pique N, Berlanga M, Minana-Galbis D . Health Benefits of Heat-Killed (Tyndallized) Probiotics: An Overview. Int J Mol Sci. 2019; 20(10). PMC: 6566317. DOI: 10.3390/ijms20102534. View

Serhan C, Savill J . Resolution of inflammation: the beginning programs the end. Nat Immunol. 2005; 6(12):1191-7. DOI: 10.1038/ni1276. View

Allouche R, Hafeez Z, Papier F, Dary-Mourot A, Genay M, Miclo L . In Vitro Anti-Inflammatory Activity of Peptides Obtained by Tryptic Shaving of Surface Proteins of LMD-9. Foods. 2022; 11(8). PMC: 9030335. DOI: 10.3390/foods11081157. View

Terzaghi B, Sandine W . Improved medium for lactic streptococci and their bacteriophages. Appl Microbiol. 1975; 29(6):807-13. PMC: 187084. DOI: 10.1128/am.29.6.807-813.1975. View

Lecomte X, Gagnaire V, Briard-Bion V, Jardin J, Lortal S, Dary A . The naturally competent strain Streptococcus thermophilus LMD-9 as a new tool to anchor heterologous proteins on the cell surface. Microb Cell Fact. 2014; 13:82. PMC: 4076053. DOI: 10.1186/1475-2859-13-82. View

Delorme C, Bartholini C, Bolotine A, Ehrlich S, Renault P . Emergence of a cell wall protease in the Streptococcus thermophilus population. Appl Environ Microbiol. 2009; 76(2):451-60. PMC: 2805209. DOI: 10.1128/AEM.01018-09. View

Henningham A, Chiarot E, Gillen C, Cole J, Rohde M, Fulde M . Conserved anchorless surface proteins as group A streptococcal vaccine candidates. J Mol Med (Berl). 2012; 90(10):1197-207. DOI: 10.1007/s00109-012-0897-9. View

10.

Kim E, Lee H, Han S, Seo K, Kim H . Effect of Surface Layer Proteins Derived from Paraprobiotic Kefir Lactic Acid Bacteria on Inflammation and High-Fat Diet-Induced Obesity. J Agric Food Chem. 2021; 69(50):15157-15164. DOI: 10.1021/acs.jafc.1c05037. View

11.

Olsen J, Ong S, Mann M . Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol Cell Proteomics. 2004; 3(6):608-14. DOI: 10.1074/mcp.T400003-MCP200. View

12.

Miclo L, Roux E, Genay M, Brusseaux E, Poirson C, Jameh N . Variability of hydrolysis of β-, αs1-, and αs2-caseins by 10 strains of Streptococcus thermophilus and resulting bioactive peptides. J Agric Food Chem. 2011; 60(2):554-65. DOI: 10.1021/jf202176d. View

13.

Guha S, Majumder K . Structural-features of food-derived bioactive peptides with anti-inflammatory activity: A brief review. J Food Biochem. 2019; 43(1):e12531. DOI: 10.1111/jfbc.12531. View

14.

Chhatwal G . Anchorless adhesins and invasins of Gram-positive bacteria: a new class of virulence factors. Trends Microbiol. 2002; 10(5):205-8. DOI: 10.1016/s0966-842x(02)02351-x. View

15.

Dandoy D, Fremaux C, Henry de Frahan M, Horvath P, Boyaval P, Hols P . The fast milk acidifying phenotype of Streptococcus thermophilus can be acquired by natural transformation of the genomic island encoding the cell-envelope proteinase PrtS. Microb Cell Fact. 2011; 10 Suppl 1:S21. PMC: 3231928. DOI: 10.1186/1475-2859-10-S1-S21. View

16.

Chakrabarti S, Guha S, Majumder K . Food-Derived Bioactive Peptides in Human Health: Challenges and Opportunities. Nutrients. 2018; 10(11). PMC: 6265732. DOI: 10.3390/nu10111738. View

17.

Tjalsma H, Lambooy L, Hermans P, Swinkels D . Shedding & shaving: disclosure of proteomic expressions on a bacterial face. Proteomics. 2008; 8(7):1415-28. DOI: 10.1002/pmic.200700550. View

18.

Samtiya M, Acharya S, Pandey K, Aluko R, Udenigwe C, Dhewa T . Production, Purification, and Potential Health Applications of Edible Seeds' Bioactive Peptides: A Concise Review. Foods. 2021; 10(11). PMC: 8621896. DOI: 10.3390/foods10112696. View

19.

Siciliano R, Lippolis R, Mazzeo M . Proteomics for the Investigation of Surface-Exposed Proteins in Probiotics. Front Nutr. 2019; 6:52. PMC: 6491629. DOI: 10.3389/fnut.2019.00052. View

20.

Li P, Yu Q, Ye X, Wang Z, Yang Q . Lactobacillus S-layer protein inhibition of Salmonella-induced reorganization of the cytoskeleton and activation of MAPK signalling pathways in Caco-2 cells. Microbiology (Reading). 2011; 157(Pt 9):2639-2646. DOI: 10.1099/mic.0.049148-0. View