Adsorption of Bacteriophages to Adhesions Between Wall and Membrane of Escherichia coli

Abstract

In plasmolyzed Escherichia coli, wall and membrane adhered to one another at 200 to 400 localized areas. This number of specialized wall areas per cell was of the same order of magnitude as the total number of bacteriophage receptors. When bacteriophages TI to T7 were adsorbed to the bacteria, they were seen to attach almost exclusively to these areas. Comparisons of the number of adsorbed phage particles observed in ultrathin sections and the expected number of phages per cell were in agreement. These results suggest a sharing of receptive areas by the various phages. Adsorption to the wall-membrane associations would permit the virus to release its nucleic acid at an area closest to the cell's protoplasmic contents. After the electron microscopic description of bacteriophage particles by Ruska (23), Luria and Anderson (17), and Luria, Delbruck, and Anderson (19), the mode of virus adsorption to surfaces of susceptible cells could be studied successfully: Anderson (2) clearly demonstrated that bacteriophages Ti and T5 adsorbed to their host cells with the tips of their tails. T-even bacteriophage adsorption involves the specific attachment of tail fibers to the bacterial receptor (13, 26, 32, 33), followed by changes in their contractile tail sheaths and baseplates (3, 14, 26, 27). However, the mode of attachment of other phage types, like T3 and T7, is still unknown (18). Extracts from bacterial envelopes contain receptor activity and function as competitive inhibitors for virus attachment to bacterial host cells (6, 16, 31). Frank, Zarnitz, and Weidel (8) showed that the deoxyribonucleic acid (DNA) of bacteriophage T5 is ejected through the tip of the tail when the particles react with receptor prepara

Transfection of Enterobacteriaceae and its applications.

“…where the inner and outer membranes appear to touch; these are the adsorption sites for many bacteriophage (22,23).…”

YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli

“…LPS transport has been suggested to proceed via putative proteinaceous contact zones between the IM and the OM (Muhlradt et al, 1973;Ishidate et al, 1986). These contact sites were first observed by Bayer (1968), and so they are often referred to as 'Bayer bridges'. LPS transport to the OM can be observed in spheroplasts of Escherichia coli, whereas phospholipid transport is not observed under the same experimental conditions (Tefsen et al, 2005).…”

Transport of vitamin B12 in Escherichia coli: common receptor system for vitamin B12 and bacteriophage BF23 on the outer membrane of the cell envelope

“…In other words, all of the receptors would be fully functional. Bayer has reported that about 5% of the outer membrane is occupied by about 200 to 400 sites of fusion to the inner membrane, and that several phage receptors, including that for BF23 (personal communication), are located predominantly at these fusion sites (1,2). Some, if not all, ofthese sites evidently participate in the insertion of nascent lipopolysaccharide into the outer membrane (15), and Leive (personal communication) found that the specific activity for B12 binding was no greater at these insertion sites than in the rest of the outer membrane.…”