A Modular High-ThroughputIn VivoScreening Platform Based on Chimeric Bacterial Receptors

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.

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Bacterial Receptors for Phages and Colicins as Constituents of Specific Transport Systems

Microbial Interactions ◽

10.1007/978-1-4615-9698-1_3 ◽

1977 ◽

pp. 99-137 ◽

Cited By ~ 7

Author(s):

V. Braun ◽

K. Hantke

Keyword(s):

Transport Systems ◽

Specific Transport ◽

Bacterial Receptors

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Adsorbed Salivary Proline-Rich Proteins as Bacterial Receptors on Apatitic Surfaces

Molecular Mechanisms of Microbial Adhesion ◽

10.1007/978-1-4612-3590-3_12 ◽

1989 ◽

pp. 143-163 ◽

Cited By ~ 18

Author(s):

R. J. Gibbons ◽

D. I. Hay

Keyword(s):

Bacterial Receptors

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Chemisorptions of bacterial receptors for hydrophobic amino acids and sugars on gold for biosensor applications: a surface plasmon resonance study of genetically engineered proteins

Biosensors and Bioelectronics ◽

10.1016/s0956-5663(03)00198-2 ◽

2003 ◽

Vol 19 (3) ◽

pp. 249-259 ◽

Cited By ~ 16

Author(s):

Linda A. Luck ◽

Michael J. Moravan ◽

John E. Garland ◽

Branka Salopek-Sondi ◽

Dipankar Roy

Keyword(s):

Amino Acids ◽

Surface Plasmon Resonance ◽

Surface Plasmon ◽

Plasmon Resonance ◽

Genetically Engineered ◽

Hydrophobic Amino Acids ◽

Biosensor Applications ◽

Engineered Proteins ◽

Bacterial Receptors

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The N-linked oligosaccharides of human lactoferrin are not required for binding to bacterial lactoferrin receptors

Canadian Journal of Microbiology ◽

10.1139/m92-198 ◽

1992 ◽

Vol 38 (11) ◽

pp. 1202-1205 ◽

Cited By ~ 12

Author(s):

J. Alcantara ◽

J. S. Padda ◽

A. B. Schryvers

Keyword(s):

Neisseria Gonorrhoeae ◽

Affinity Chromatography ◽

Neisseria Meningitidis ◽

Key Words ◽

Concanavalin A ◽

Moraxella Catarrhalis ◽

Competitive Binding ◽

Human Lactoferrin ◽

Bacterial Receptors

The oligosaccharides of human lactoferrin were enzymatically removed with glycopeptidase F, resulting in a preparation containing partial and fully deglycosylated human lactoferrin. The derivatives were separated by Concanavalin A affinity chromatography and compared with native human lactoferrin with respect to their ability to bind to bacterial receptors. Competitive binding experiments demonstrated that the lactoferrin derivatives were equally capable as native lactoferrin in binding to receptors of Neisseria meningitidis, Neisseria gonorrhoeae, and Moraxella catarrhalis. This result indicates that the oligosaccharides on human lactoferrin are not essential for binding to the bacterial receptors. Key words: lactoferrin, oligosaccharides, deglycosylation, receptor, Neisseria.

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