At pH 7 the bacteriophages T1 and T2 attach to anionic exchangers when suspended either in distilled water or in salt solutions. They attach to cationic exchangers only in the presence of salt. T2 requires approximately ten times higher a salt concentration than does T1 virus, a relationship which is duplicated in the attachment of these phages to their common host cell, E. coli B.
The host cell, E. coli B, attaches to anionic exchangers when suspended either in salt or distilled water, but does not attach to cationic exchangers even in 0.2 M NaCl.
These observations support the hypothesis previously advanced that the role of cations in effecting union of viruses to their host cells is to neutralize the repulsive electrostatic potential due to the excess of negative charges on the surfaces of both bodies.
Influenza virus similarly requires salt for attachment to cationic exchangers, and unites to anionic exchangers even in the absence of salt. It is therefore proposed that the same general principles which govern the behavior of the bacteriophage system, may also apply to host cell attachment of at least some mammalian viruses.
T1 bacteriophage and influenza virus are readily eluted from cationic exchangers. T2 bacteriophage cannot be recovered in active form.
Experiments with P32- and S35-labelled T2 bacteriophage reveal that shortly after its attachment to the resin, the virus is split into its phosphorus-containing DNA, and the sulfur-containing protein fraction.
It is proposed that the splitting of phage into its protein and DNA components that occurs ordinarily at the surface of a cell is a result of the establishment of the primary electrostatic bonds, just as in the attachment to cationic exchange resins.
The affinity of cationic resins for influenza virus is great enough to remove the virus almost completely from red cells to which it has become attached.