A comparative study of the fine antigen structure of phage DDVI and its h mutant using neutralization reaction and the electron microscopy of the phage-antibody complex has shown that the head and the tail of these phages have common protein constituents. The bulk of the antigens located in tail's fibers and in a base plates is also identical. However, the application of the cross-adsorbed sera has shown that the phage DDVI and the h mutant differ by only one specific antigen located in the distal part of tail's fibers.
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Biophys Chem
October 2006
Department of Exact and Natural Sciences, Tbilisi State University, Tbilisi, 0128, Georgia Country.
Knowledge of both the packaging of the linear, double-stranded (ds)DNA in bacteriophages and its subsequent release into the bacterial host is vital to our understanding of phage infection. There is now strong evidence that packaging requires a powerful rotary motor fuelled by ATP. From thermodynamic studies, however, it has been proposed that, at least for those viruses with a contractile tail, the dsDNA ejection from the phage head is a relatively simple physical process that does not require cellular energy and is facilitated by the difference in the conditions of the medium in the environments inside and outside the head.
View Article and Find Full Text PDFA brief review of literature data and our investigations on the antibodies used for specific labeling in electron microscopy is presented. Considered are the problems connected with structure and function of separate components of bacterial viruses revealed by means of specific antibodies. The results of fine differentiation of antigenic components in the case of phages of the colidysentery group allowed to elucidate the functional role of the adsorption apparatus in the course of phage interaction with the bacterial cell.
View Article and Find Full Text PDFTopology of the products of the genes 34, 35, 36 and 37 of the bacteriophage T4D long tail fibers were determined with the aid of monospecific antibodies. The antibodies against gene product 34 were the only to interact with the proximal part of long tail fibers, but the distal part bound the antibodies against 35, 36 and 37. Product of the gene 35 is located at the joint-site with the distal part and binds the distance not more than 75 A long.
View Article and Find Full Text PDFSome interaction process peculiarites of morphologically related phate T4, DDVI and FI1 with the corresponding antiphageous sera in cross reactions of neutralisation have been investigated. Close serological relationship of phage T4 and DDVI was demonstrated. Inactivation of phage FI1 in these serological reactions showed anomalous nature and did not submit to the rules of the first step reaction.
View Article and Find Full Text PDFBiochim Biophys Acta
January 1979
DNA methylase methylating adenine with formation of 6-methylaminopurine has been identified in Shigella sonnei 1188 cells which are the natural host of DDVI phage. At the same time, in DNA of DDVI phage replicating both in Sh. sonnei 1188 cells and in Escherichia coli B cells 7-methylguanine was found as the only minor base in amounts of 0.
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