FEMS immunology and medical microbiology最新文献

{"title":"In vitro and in silico analysis of signal peptides from the human blood fluke, Schistosoma mansoni","authors":"Mark S. Pearson ,&nbsp;Donald P. McManus ,&nbsp;Danielle J. Smyth ,&nbsp;Fred A. Lewis ,&nbsp;Alex Loukas","doi":"10.1016/j.femsim.2005.03.009","DOIUrl":"10.1016/j.femsim.2005.03.009","url":null,"abstract":"<div><p><span>Proteins secreted by and anchored on the surfaces of parasites are in intimate contact with host tissues. The transcriptome of infective cercariae of the blood fluke, </span><span><em>Schistosoma mansoni</em></span><span><span>, was screened using signal sequence<span> trap to isolate cDNAs encoding predicted proteins with an N-terminal signal peptide. Twenty cDNA fragments were identified, most of which contained predicted signal peptides or transmembrane regions, including a novel putative seven-transmembrane receptor and a membrane-associated mitogen-activated protein kinase. The developmental expression pattern within different life-cycle stages ranged from ubiquitous to a transcript that was highly upregulated in the cercaria. A bioinformatics-based comparison of 100 signal peptides from each of schistosomes, humans, a </span></span>parasitic nematode and </span><em>Escherichia coli</em><span> showed that differences in the sequence composition of signal peptides, notably the residues flanking the predicted cleavage site, might account for the negative bias exhibited in the processing of schistosome signal peptides in mammalian cells.</span></p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.03.009","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25218424","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Major structural proteins of type 1 and type 3 Klebsiella fimbriae are effective protein carriers and immunogens in conjugates as revealed from their immunochemical characterization","authors":"Danuta Witkowska ,&nbsp;Małgorzata Mieszała ,&nbsp;Andrzej Gamian ,&nbsp;Magdalena Staniszewska ,&nbsp;Anna Czarny ,&nbsp;Anna Przondo-Mordarska ,&nbsp;Michel Jaquinod ,&nbsp;Eric Forest","doi":"10.1016/j.femsim.2005.04.005","DOIUrl":"10.1016/j.femsim.2005.04.005","url":null,"abstract":"<div><p><span>Fimbriae are filamentous structures present on the cell surface of many bacteria, including genus </span><span><em>Klebsiella</em></span><span>. The use of fimbriae as protein carriers in conjugates may allow to formulate effective multivalent vaccines and suitable diagnostics. However, the evidences have been reported that fimbriae may enhance the inflammatory response. This prompted us to examine the degree of cytokine induction by the type 1 and type 3 </span><em>Klebsiella</em> fimbriae and their conjugates. Fimbriae were assessed as carrier proteins for <em>Escherichia coli</em><span><span> K12 endotoxin core </span>oligosaccharide<span>. MALDI-MS revealed the molecular mass of fimbrial monomer major protein, which was 15,847 Da for type 1 and 18,574 Da for type 3 fimbriae of </span></span><em>Klebsiella</em><span>. These two types of fimbriae were moderate inductors of IL-6 and interferon and almost inactive with regard to the stimulation of TNF when tested in human whole blood assay. Coupling of fimbriae with </span><em>E. coli</em><span><span><span> K12 core oligosaccharide gave immunogenic conjugates with respect to a saccharide ligand and protein carrier, although only 10% of the pilin<span> monomers possessed the attached oligosaccharide. Rabbit antiserum reacted with a broad spectrum of </span></span>lipopolysaccharides, as measured by </span>ELISA<span> and immunoblotting<span> assays. The antibodies against glycoconjugates were bactericidal for the wild, S-type bacteria of some species. Regarding the induction of cytokines by conjugates only the TNF level was noticeably elevated. These results prompt for the practical use of fimbriae, as effective protein carriers for conjugates to obtain broad-spectrum antisera for diagnostic applications.</span></span></span></p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.04.005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25131050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification and characterization of a novel fibronectin-binding protein gene from Streptococcus equi subspecies zooepidemicus strain VTU211","authors":"Kyongsu Hong","doi":"10.1016/j.femsim.2005.04.006","DOIUrl":"10.1016/j.femsim.2005.04.006","url":null,"abstract":"<div><p>This work describes the cloning and sequencing of genes encoding fibronectin-binding proteins from <span><em>Streptococcus equi</em></span> subspecies <em>zooepidemicus</em><span> strain VTU211. A gene encoding a cell-wall protein FNZ was amplified and sequenced. In the same bacterial strain, a second gene termed </span><em>fnz2</em><span> was now discovered, encoding another fibronectin-binding protein (FNZ2). The complete amino acid sequence encoded by </span><em>fnz2</em> was deduced and compared to that deduced from <em>fnz</em>. The sequence comparison of the <em>fnz</em> and <em>fnz2</em><span> predicted that fibronectin-binding activity is localizing a domain in the C terminal part of FNZ2, since this domain is composed of three repeats, which contain a motif similar to what has earlier been found in other fibronectin-binding proteins in streptococci. Three parts of </span><em>fnz2</em> [<em>fnz2</em>(<em>1</em>-<em>8</em>), <em>fnz2</em>(<em>2</em>-<em>4</em>), and <em>fnz2</em>(<em>4</em>-<em>3</em><span><span>)] were amplified using polymerase chain reaction and ligated into an </span>expression vector, and recombinant FNZ2 proteins were produced in </span><em>Escherichia coli</em><span>. Fibronectin bound to the FNZ2(1-8) [amino acids 212–396] and FNZ2(2-4) (amino acids 36–448) but not to the FNZ2(4-3) (amino acids 36–191) in a Western ligand blot, showing that repeat domain of FNZ2 protein was sufficient for binding of fibronectin. Purified FNZ2(2-4) protein was also shown to display collagen-binding activity to collagen-coated microtiter wells. These results show that recombinant FNZ2 has fibronectin- and collagen-binding activities.</span></p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.04.006","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25131570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Relationship of HIV RNA and cytokines in saliva from HIV-infected individuals","authors":"Gregory T. Spear ,&nbsp;Mario E.A.F. Alves ,&nbsp;Mardge H. Cohen ,&nbsp;James Bremer ,&nbsp;Alan L. Landay","doi":"10.1016/j.femsim.2005.03.002","DOIUrl":"10.1016/j.femsim.2005.03.002","url":null,"abstract":"<div><p><span>We measured levels of six cytokines and human immunodeficiency virus (HIV) RNA in saliva from HIV-seropositive individuals and compared salivary cytokine levels in HIV-seropositives and seronegatives. All of the six tested cytokines were detected in saliva although interleukin-1β, interferon-γ and interleukin-10 were detected more frequently (90%, 68% and 61% of samples, respectively) than interleukin-6, tumor necrosis factor-α and tumor necrosis factor-α receptor II (2–17%). There was no significant association between cytokine levels in saliva and plasma suggesting that cytokines were produced locally. Interferon-γ levels were significantly higher in saliva from HIV-seropositives when compared to seronegatives while interleukin-10 levels were lower in seropositive saliva. Interleukin-10 levels were higher in individuals with low CD4 counts in the seropositive group. HIV RNA was detected in 29% of saliva samples from seropositives and there was a significant correlation between saliva and plasma HIV RNA levels. However, HIV RNA levels in saliva were not significantly associated with any of the saliva or plasma cytokine levels or with CD4 cell numbers. This study shows no association between inflammatory cytokine levels and HIV levels in saliva and suggests that saliva HIV levels are more influenced by blood HIV RNA levels than </span>oral inflammation.</p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.03.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25218516","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rapid molecular identification of Neisseria meningitidis isolates using the polymerase chain reaction followed by single-stranded conformation polymorphism analysis","authors":"Konstantinos Kesanopoulos ,&nbsp;Georgina Tzanakaki ,&nbsp;Aristea Velegraki ,&nbsp;Nikolaos Tegos ,&nbsp;Dominique A. Caugant ,&nbsp;Panagiotis Menounos ,&nbsp;Jenny Kourea-Kremastinou ,&nbsp;Stamatina Levidiotou-Stefanou","doi":"10.1016/j.femsim.2005.03.003","DOIUrl":"10.1016/j.femsim.2005.03.003","url":null,"abstract":"<div><p>Typing of <span><em>Neisseria meningitidis</em></span><span> strains is currently performed with conventional and molecular methods. Our objectives were: first, to develop a polymerase chain reaction (PCR) followed by single-stranded conformation polymorphism (SSCP) analysis of the </span><em>Por</em>A gene (VR1 region) to distinguish <em>N. meningitidis</em> subtypes and second, to evaluate the method for the identification and characterization of <em>N. meningitidis</em> in patient specimens. SSCP analysis of the VR1 region of the <em>Por</em>A1/2 gene from 126 <em>N. meningitidis</em><span> strains and 29 clinical samples identified seven SSCP types (SP-1 to SP-7); four strains were not typeable by the method. Classification according to the SSCP methods and serosubtype agreed for 122 of the 126 typeable strains (96.8%). For the 24-culture positive clinical samples, serosubtype and SSCP agreed in all cases. Five samples, which were culture-negative but obtained from children during an apparent outbreak of meningococcal disease in a primary school, presented identical SSCP classification for each sample (SP-2). PCR-SSCP is a rapid and cost-effective method for typing </span><em>N. meningitidis</em> strains that could provide important early information in the surveillance of suspected meningococcal outbreaks, particularly when culture-negative specimens constitutes the main source of material to analyze.</p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.03.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25218518","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Efficacy of non-toxic deletion mutants of protective antigen from Bacillus anthracis","authors":"Gi-eun Rhie ,&nbsp;Young-Mia Park ,&nbsp;Ji-Sun Han,&nbsp;Jae-Yon Yu,&nbsp;Won-Keun Seong,&nbsp;Hee-Bok Oh","doi":"10.1016/j.femsim.2005.05.009","DOIUrl":"10.1016/j.femsim.2005.05.009","url":null,"abstract":"<div><p>Current human anthrax vaccines available in the United States and Europe consist of alum-precipitated supernatant material from cultures of a toxigenic, nonencapsulated strain of <em>Bacillus anthracis</em>. The major component of human anthrax vaccine that confers protection is protective antigen (PA). A second-generation human vaccine using the recombinant PA (rPA) is being developed. In this study, to prevent the toxicity and the degradation of the native rPA by proteases, we constructed two PA variants, delPA (163–168) and delPA (313–314), that lack trypsin (S¹⁶³–<u>R¹⁶⁴–K¹⁶⁵–K¹⁶⁶–R¹⁶⁷</u>–S¹⁶⁸) or chymotrypsin cleavage sequence (<u>F³¹³–F³¹⁴</u>), respectively. These proteins were expressed in <em>Bacillus brevis</em> 47-5Q. The delPAs were fractionated from the culture supernatant of <em>B. brevis</em> by ammonium sulfate at 70% saturation, followed by anion exchange chromatography on a Hitrap Q, Hiload 16/60 superdex 200 gel filtration column and phenyl sepharose hydrophobic interaction column. In accordance with previous reports, both delPA proteins combined with lethal factor protein did not show any cytotoxicity on J774A.1 cells. The delPA (163–168) and delPA (313–314) formulated either in Rehydragel HPA or MPL-TDM-CWS (Ribi-Trimix), elicited a comparable amount of anti-PA and neutralizing antibodies to those of native rPA in guinea pigs, and confers full protection of guinea pigs from 50<!--> <!-->×<!--> <!-->LD₅₀ of fully virulent <em>B. anthracis</em> spore challenges. Ribi-Trimix was significantly more effective in inducing anti-PA and neutralizing antibodies than Rehydragel HPA. These results indicate the possibility of delPA (163–168) and delPA (313–314) proteins being developed into nontoxic, effective and stable recombinant vaccine candidates.</p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.05.009","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25191387","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Brucella melitensis infection associated with Guillain–Barré syndrome through molecular mimicry of host structures","authors":"Kenta Watanabe ,&nbsp;Suk Kim ,&nbsp;Megumi Nishiguchi ,&nbsp;Hiroshi Suzuki ,&nbsp;Masahisa Watarai","doi":"10.1016/j.femsim.2005.03.001","DOIUrl":"10.1016/j.femsim.2005.03.001","url":null,"abstract":"<div><p><span><em>Brucella melitensis</em></span><span> is a facultative intracellular bacterium<span> that can survive inside macrophages and the causative agent of brucellosis<span>. In the present study, we found that a lipooligosaccharide of </span></span></span><em>B. melitensis</em><span><span> has a GM1 ganglioside-like structure and shows a strong antibody response in mice. The </span>cholera toxin B subunit<span>, which binds to GM1 ganglioside specifically, reacted with the surface of </span></span><em>B. melitensis</em>. Immunization with <em>B. melitensis</em> induced the production of anti-GM1 ganglioside antibodies in mice and serum from immunized mice showed a cross-reaction with Guillain–Barré syndrome (GBS)-associated <span><em>Campylobacter jejuni</em></span>, but not non-GBS-associated <em>C. jejuni</em>. When <em>B. melitensis</em><span> was treated with a neuraminidase, antibody responses disappeared. </span><em>B. melitensis</em> immunization induced the production of anti-GM1 ganglioside antibodies in BALB/c mice but not in C57BL/6 and ddY mice, and for BALB/c mice, immunization with <em>B. melitensis</em> induced much greater production of anti-GM1 ganglioside than GBS-associated <em>C. jejuni</em>. Flaccid limb weakness was observed in <em>B. melitensis</em> immunized mice. These results suggest that <em>B. melitensis</em> is a new etiological agent for GBS and that immunological responses between it and GBS-associated <em>C. jejuni</em> in the mouse model may be different.</p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.03.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25218515","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Distinct bacterial dissemination and disease outcome in mice subcutaneously infected with Borrelia burgdorferi in the midline of the back and the footpad","authors":"Amir-Reza T. Motameni,&nbsp;Tonya C. Bates,&nbsp;Ignacio J. Juncadella,&nbsp;Cynthia Petty,&nbsp;Michael N. Hedrick,&nbsp;Juan Anguita","doi":"10.1016/j.femsim.2005.05.001","DOIUrl":"10.1016/j.femsim.2005.05.001","url":null,"abstract":"<div><p>Subcutaneous inoculation of mice with <span><em>Borrelia burgdorferi</em></span><span><span>, the causative agent of Lyme disease, results in established infection and the development of acute arthritis and </span>carditis<span>, hallmarks of human disease. Because conflicting results may originate from the site of subcutaneous inoculation, we addressed the dissemination capacity of spirochetes injected in the shoulder region versus the footpad. Spirochetes inoculated in the footpad disseminated to a lesser extent to distant organs, such as the ear and the heart. This resulted in distinct degrees of joint and cardiac inflammation at the peak of the disease. The differences eventually leveled out. These results suggest that caution must be exercised in the interpretation of results obtained with routes of inoculation that do not closely represent the natural site of infection.</span></span></p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.05.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25131573","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structures of the biological repeating units in the O-chain polysaccharides of Hafnia alvei strains having a typical lipopolysaccharide outer core region","authors":"Ewa Katzenellenbogen ,&nbsp;Nina A. Kocharova ,&nbsp;George V. Zatonsky ,&nbsp;Alexander S. Shashkov ,&nbsp;Maria Bogulska ,&nbsp;Yuriy A. Knirel","doi":"10.1016/j.femsim.2005.05.003","DOIUrl":"10.1016/j.femsim.2005.05.003","url":null,"abstract":"<div><p><span>Earlier, the structures of the O-chain polysaccharides<span> of the lipopolysaccharides (LPS) of a number of </span></span><span><em>Hafnia </em><em>alvei</em></span><span><span> strains have been established. However, it remained unknown, which is the first and the last monosaccharide of the O-chain. This is defined by the structure of the so-called biological repeating unit (O-unit), which is pre-assembled and then polymerised in the course of biosynthesis of </span>bacterial polysaccharides by the Wzy-dependent pathway. Now we report on the structures of the O-units in 10 </span><em>H. alvei</em><span><span> strains. The LPS were cleaved by mild acid hydrolysis and oligosaccharide fractions IIIa and IIIb were isolated by gel chromatography subsequently on </span>Sephadex<span> G-50 and BioGel P-2 and studied by methylation<span> analysis and NMR spectroscopy. Fraction IIIb was found to represent the core oligosaccharide containing a terminal upstream α-</span></span></span><span>d</span>-Glc-(1→3)-α-<span>d-</span>Glc or α-<span>d</span>-Gal-(1→3)-α-<span>d-G</span><span>lc disaccharide in the outer region that is typical of </span><em>H. alvei</em>. Fraction IIIa consists of the LPS core with one O-unit linked by a 3-substituted β-<span>d</span>-GalNAc residue (in strains PCM 1189 and PCM 1546) or a 3-substituted β-<span>d</span>-GlcNAc residue (in the other strains studied). In most strains examined the β-configuration of the <span>d</span>-GlcNAc linkage in the first O-unit attached to the core is the same and in some strains is opposite to that found in the interior O-units of the O-chain polysaccharide. Various monosaccharides, including <span>d</span>-Glc, <span>d</span>-Gal, <span>d</span>-GlcA and acyl derivatives of 3-amino-3,6-dideoxy-<span>d</span>-glucose or 4-amino-4,6-dideoxy-<span>d</span>-glucose, occupy the non-reducing end of the O-unit.</p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.05.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25140521","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Oral probiotic bacterial administration suppressed allergic responses in an ovalbumin-induced allergy mouse model","authors":"Hyeyoung Kim ,&nbsp;Kubum Kwack ,&nbsp;Dae-Young Kim ,&nbsp;Geun Eog Ji","doi":"10.1016/j.femsim.2005.05.005","DOIUrl":"10.1016/j.femsim.2005.05.005","url":null,"abstract":"<div><p><span>This study investigated whether orally administered probiotic bacteria (</span><span><em>Bifidobacterium bifidum</em></span> and <span><em>Lactobacillus casei</em></span>) and a gram-negative bacterium (<em>Escherichia coli</em><span><span><span>) function as allergic immune modulators to prevent food allergy, according to the </span>hygiene hypothesis<span><span>. C3H/HeJ mice were sensitized with ovalbumin (OVA) and </span>cholera toxin for 5 weeks. After sensitization, the OVA-induced mice that were not treated with bacteria had significantly increased levels of OVA-specific IgE, total IgE, and </span></span>IgG1 in sera, as well as scab-covered tails. In comparison, groups treated with </span><em>B. bifidum</em> BGN4 (BGN4), <em>L. casei</em> 911 (<em>L. casei</em>), or <em>Escherichia coli</em> MC4100 (<em>E. coli</em><span>) had decreased levels of OVA-specific IgE, total IgE, and IgG1, and decreased levels of mast cell degranulation and tail scabs. OVA-specific IgA levels were decreased in BGN4- and </span><em>L. casei</em>-treated groups. In conclusion, administration of <em>E. coli</em>, BGN4, or <em>L. casei</em> decreased the OVA-induced allergy response. However, a normal increase in body weight was inhibited in the <em>E. coli</em>-treated mice and in the montreated mice groups during allergy sensitization. Thus, BGN4 and <em>L. casei</em> appear to be useful probiotic bacteria for the prevention of allergy.</p></div>","PeriodicalId":12220,"journal":{"name":"FEMS immunology and medical microbiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2005-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.femsim.2005.05.005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25142685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}