Bacteriophage receptors

The stability of the /3-barrel itself was demonstrated in engineering experiments with OmpA. The four external loops of OmpA were replaced by shortcuts in all possible combinations (Koebnik, 1999). The resulting deletion mutants lost their biological functions in bacterial / -conjugation and as bacteriophage receptors, but kept the transmembrane /1-barrel as demonstrated by their resistance to proteolysis and thermal denaturation. The results confirm the expectation that the large external loops do not contribute to /1-barrel folding and stability. 

Morona, R., Klose, M., and Henning, U. (1984). Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage receptor analysis of mutant genes expressing altered proteins. / Baderiol. 159, 570-578. 

The biological properties associated with the polysaccharides are those relating to serological specificity, and, at least to some extent, they serve as bacteriophage receptors. The somatic antigens are also referred to as Endotoxins, but their toxic properties and manifold physiological effects are due to the lipide component, and this subject has been adequately reviewed. ... 

A number of rough mutants obtained from Sh. flexneri and related bacteriophage receptors have been classified into chemotypes based on chemical analysis of the lipopolysaccharides. The results suggest that all Sh. flexneri serotypes contain a common core. The receptor sites for several bacteriophages have been found to vary from the entire core structure of the lipopolysaccharide to a single monosaccharide residue. 

Spinelli, S., Desmyter, A., Verrips, G. T., de Haard, H. J., Moineau, S., and Cambillau, C. (2006). Lactococcal bacteriophage P2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat. Struct. Mol. Biol. 13, 85-89. 

Thomassen, E., Gielen, G., Schutz, M., Schoehn, G., Abrahams, J. P., Miller, S., and van Raaij, M. J. (2003). The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. J. Mol. Biol. 331, 361-373. 

Wang,J., Hofnung, M., and Charbit, A. (2000). The C-terminal portion of the tail fiber protein of bacteriophage lambda is responsible for binding to LamB, its receptor at the surface of Escherichia coli K-12./. Bacteriol. 182, 508-512. 

Fig. 5.1 Schematic drawing of membrane association modes of peptides A Integral membrane proteins (1) major fd coat protein gpVIII of bacteriophage Ml 3 (pdb lfdm), anchored by an 18-residue trans-membrane hydrophobic helix (2) bovine rhodopsin, a 7 trans-membrane domain (G-protein-coupled) receptor (pdb lf88) (3) ion channel peptaibol Chrysospermin C (pdb lee7), and B Peripheral membrane proteins (1) neuro-...

The first step in bacteriophage infection is the adsorption of the phage to a receptor on the bacterium. Almost every structure on the surface of a bacterial cell, or extending from it, can act as (or include) phage receptors (29). The 0-antigenic polysaccharide chains of the LPS are no exgeption in this respect. Since it has been estimated that 10 > to 10 LPS molecules are found on each bacterial cell (30), it is evident that part of the... 

The exterior surface of Gram-positive bacteria is covered by teichoic acids. These are ribitol-phosphate or glycerol-phosphate polymer chains that are frequently substituted by alanine and glycosidically linked monosaccharides (Figure A2.4). They are attached to the peptidoglycan by a phosphate diester link. Teichoic acids can act as receptors to bacteriophages and some appear to have antigenic properties. 

Li M, Use of a modified bacteriophage to probe the interactions between peptides and ion channel receptors in mammalian cells, Nat. Biotechnol., 15 559-563, 1997. 

Goodson RJ, Doyle MV, Kaufman SE, Rosenberg S, High-affinity urokinase receptor antagonists identified with bacteriophage peptide display, Proc. Natl. Acad. Sci. USA, 91 7129-7133, 1994. 

---