S9A Serine Protease Engender Antigenic Gluten Catabolic Competence to the Human Gut Microbe

TY - JOUR

T1 - S9A Serine Protease Engender Antigenic Gluten Catabolic Competence to the Human Gut Microbe

AU - Kumar, Jitendra

AU - Verma, Manoj Kumar

AU - Kumar, Tarun

AU - Gupta, Shashank

AU - Pandey, Rajesh

AU - Yadav, Monika

AU - Chauhan, Nar Singh

PY - 2018/9/1

Y1 - 2018/9/1

N2 - The human gut microbiome has a significant role in host physiology; however its role in gluten catabolism is debatable. Present study explores the role of human gut microbes in gluten catabolism and a native human gut microbe Cellulomonas sp. HM71 was identified. SSU rDNA analysis has described human gut microbiome structure and also confirmed the permanent residentship of Cellulomonas sp. HM71. Catabolic potential of Cellulomonas sp. HM71 to cleave antigenic gluten peptides indicates presence of candidate gene encoding biocatalytic machinery. Genome analysis has identified the presence of gene encoding S9A serine protease family-prolyl endopeptidase, with Ser591, Asp664 and His685 signature residues. Cellulomonas sp. HM71 prolyl endopeptidase activity was found optimal at pH 7.0 and 37 °C with a K M of 35.53 μmol and specifically cleaves at proline residue. Current study describes the gluten catabolism potential of Cellulomonas sp. HM71 depicting possible role of human gut microbes in gluten catabolism to confer resistance mechanisms for the onset of celiac diseases in populations with gluten diet.

AB - The human gut microbiome has a significant role in host physiology; however its role in gluten catabolism is debatable. Present study explores the role of human gut microbes in gluten catabolism and a native human gut microbe Cellulomonas sp. HM71 was identified. SSU rDNA analysis has described human gut microbiome structure and also confirmed the permanent residentship of Cellulomonas sp. HM71. Catabolic potential of Cellulomonas sp. HM71 to cleave antigenic gluten peptides indicates presence of candidate gene encoding biocatalytic machinery. Genome analysis has identified the presence of gene encoding S9A serine protease family-prolyl endopeptidase, with Ser591, Asp664 and His685 signature residues. Cellulomonas sp. HM71 prolyl endopeptidase activity was found optimal at pH 7.0 and 37 °C with a K M of 35.53 μmol and specifically cleaves at proline residue. Current study describes the gluten catabolism potential of Cellulomonas sp. HM71 depicting possible role of human gut microbes in gluten catabolism to confer resistance mechanisms for the onset of celiac diseases in populations with gluten diet.

U2 - 10.1007/s12088-018-0732-2

DO - 10.1007/s12088-018-0732-2

M3 - Journal article

C2 - 30013273

SN - 0046-8991

VL - 58

SP - 294

EP - 300

JO - Indian Journal of Microbiology

JF - Indian Journal of Microbiology

IS - 3

ER -