title: Differential effect of Bacillus firmus on immune response and enterocyte brush-border enzyme levels in BALB/c and B10.BR mice.
abstract: A nonpathogenic bacterium of external environment possessing remarkable immunomodulatory activity, Bacillus firmus (BF) inactivated with formaldehyde, was given intragastrically to two genetically different mouse strains BALB/c (H-2d) and B10.BR/SnPh (B10.BR, H-2k) reared in conventional (CV) and B10.BR strain also in germ-free (GF) conditions. Repeated intragastric administration of BF (500 micrograms every other day over two weeks, starting at the age of 3 months) significantly enhanced intestinal IgA levels in CV BALB/c mice but did not affect intestinal IgA in CV B10.BR mice. In GF B10.BR mice, IgG levels in sera and intestinal washings increased after BF administration compared to CV B10.BR mice. In CV BALB/c mice, specific activity of enterocyte brush-border enzymes (lactase, gamma-glutamyltransferase, alkaline phosphatase) decreased after BF treatment; sucrase (sucrose alpha-glucosidase) activity was not affected. On the other hand, in B10.BR mice, specific activity of gamma-glutamyltransferase and dipeptidyl peptidase IV were higher after administration of BF in both CV and GF groups relative to untreated controls. The activities of lactase and glucoamylase (glucan 1,4-alpha-glucosidase) were significantly stimulated only in the group of GF B10.BR mice treated with formolized BF. The stimulation of immunoglobulin production after BF treatment was accompanied by changes in the levels of enterocyte brush-border enzymes; this responsiveness to BF treatment was genetically regulated.
authors.affiliation: Department of Immunology and Gnotobiology, Institute of Microbiology, Academy of Sciences of the Czech Republic, 549 22 Nový Hrádek, Czechia. kozakova.hana@seznam.cz
authors.forename: H
authors.initials: H
authors.lastname: Kozáková
authors.forename: P
authors.initials: P
authors.lastname: Mlcková
authors.forename: J
authors.initials: J
authors.lastname: Kolínská
authors.forename: D
authors.initials: D
authors.lastname: Cechová
authors.forename: R
authors.initials: R
authors.lastname: Stĕpánková
authors.forename: Z
authors.initials: Z
authors.lastname: Reháková
authors.forename: L
authors.initials: L
authors.lastname: Prokesová
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D001407:Bacillus / Q000276:immunology*; D018819:Dipeptidyl Peptidase 4 / Q000378:metabolism; D020895:Enterocytes / Q000201:enzymology / Q000382:microbiology; D005260:Female; D020022:Genetic Predisposition to Disease; D005856:Germ-Free Life; D005087:Glucan 1,4-alpha-Glucosidase / Q000378:metabolism; D007070:Immunoglobulin A / Q000096:biosynthesis / Q000097:blood; D007150:Immunohistochemistry; D007413:Intestinal Mucosa / Q000201:enzymology / Q000276:immunology / Q000382:microbiology; D007422:Intestines / Q000201:enzymology / Q000276:immunology* / Q000382:microbiology*; D043322:Lactase; D051379:Mice; D008807:Mice, Inbred BALB C; D008871:Microvilli / Q000201:enzymology; D013393:Sucrase / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism
chemical_list: D007070:Immunoglobulin A; D000469:Alkaline Phosphatase; D043322:Lactase; D001616:beta-Galactosidase; D005087:Glucan 1,4-alpha-Glucosidase; D013393:Sucrase; D018819:Dipeptidyl Peptidase 4