Výsledky vyhledávání - "Pouwels, P.h."

Akademický článek

Chapter 15 Development of lactobacilli for mucosal immunization

Autor: Seegers, J.F.M.L., Havenith, C.E.G., Kremer, S.H.A., Pouwels, P.H.

Publikováno v: In Biology of Growing Animals 2005 2:328-350

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Akademický článek

Cell surface hydrophobicity is conveyed by S-layer proteins—a study in recombinant lactobacilli

Autor: van der Mei, H.C ^*, van de Belt-Gritter, B, Pouwels, P.H, Martinez, B, Busscher, H.J

Publikováno v: In Colloids and Surfaces B: Biointerfaces 2003 28(2):127-134

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Lactobacilli expressing variable domain of llama heavy-chain antibody fragments (lactobodies) confer protection against rotavirus-induced diarrhea

Autor: Pant, N., Hultberg, A., Zhao, Y., Svensson, L., Pan-Hammarström, Q., Johansen, K., Pouwels, P.H., Ruggeri, F.M., Hermans, P., Frenken, L., Borén, T., Marcotte, H., Hammarström, L.

Publikováno v: Journal of Infectious Diseases, 11, 194, 1580-1588

Background. Rotavirus-induced diarrhea poses a worldwide medical problem in causing substantial morbidity and mortality among children in developing countries. We therefore developed a system for passive immunotherapy in which recombinant lactobacill

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Expression of the xylulose 5-phosphate phosphoketolase gene, xpkA, from Lactobacillus pentosus MD363 is induced by sugars that are fermented via the phosphoketolase pathway and is repressed by glucose mediated by CcpA and the mannose phosphoenolpyruvate phosphotransferase system

Autor: Posthuma, C.C., Bader, R., Engelmann, R., Postma, P.W., Hengstenberg, W., Pouwels, P.H.

Publikováno v: Applied and Environmental Microbiology, 2, 68, 831-837

Purification of xylulose 5-phosphate phosphoketolase (XpkA), the central enzyme of the phosphoketolase pathway (PKP) in lactic acid bacteria, and cloning and sequence analysis of the encoding gene, xpkA, from Lactobacillus pentosus MD363 are describe

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One repeat of the cell wall binding domain is sufficient for anchoring the Lactobacillus acidophilus surface layer protein

Autor: Smit, E., Pouwels, P.H.

Publikováno v: Journal of Bacteriology, 16, 184, 4617-4619

The N-terminal repeat (SAC1) of the S-protein of Lactobacillus acidophilus bound efficiently and specifically to cell wall fragments (CWFs) when fused to green fluorescent protein, whereas the C-terminal repeat (SAC2) did not. Treatment of CWFs with

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Structural and functional analysis of the S-layer protein crystallisation domain of Lactobacillus acidophilus ATCC 4356 : evidence for protein : protein interaction of two subdomains

Autor: Smit, E., Jager, D., Martinez, B., Tielen, F.J., Pouwels, P.H.

Publikováno v: Journal of Molecular Biology, 5, 324, 953-964

The structure of the crystallisation domain, SAN, of the S A-protein of Lactobacillus acidophilus ATCC 4356 was analysed by insertion and deletion mutagenesis, and by proteolytic treatment. Mutant S A-protein synthesised in Escherichia coli with 7-13

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The S-layer protein of Lactobacillus acidophilus ATCC 4356 : identification and characterisation of domains responsible for S-protein assembly and cell wall binding

Autor: Smit, E., Oling, F., Demel, R., Martinez, B., Pouwels, P.H.

Publikováno v: Journal of Molecular Biology, 2, 305, 245-257

Lactobacillus acidophilus, like many other bacteria, harbors a surface layer consisting of a protein (SA-protein) of 43 kDa. SA-protein could be readily extracted and crystallized in vitro into large crystalline patches on lipid monolayers with a net

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