Structural proteins of the Actinobacillus actinomycetemcomitans bacteriophage øAa

R. H. Stevens, B. F. Hammond, D. H. Fine

Research output: Contribution to journalArticle

6 Scopus citations


Aa is an A 1 morphotype bacteriophage which infects certain strains of Actino bacillus actinomycetemcomitans. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) analysis of dissociated, purified ØAa particles revealed 7 major structural proteins (P1‐P7) ranging in size from 17.5 to 52.7 kilodaltons (Kd). Treatment of the intact phage particles with 67% dimethyl sulfoxide (DMSO) resulted in the separation of the virion head and tail subunits. Purification of the head subunits was accomplished by sucrose density gradient centrifugation of the DMSO‐treated phage particles. The purified head subunits were composed of a single protein having an electrophoretic mobility which corresponded to a 39.5 Kd protein (P3) of the intact virus. Raising the pH of a purified 0Aa suspension to 12.7 disrupted the head subunits, as well as the tail tube and tail fibers, releasing intact contractile tail sheaths. The tail sheaths were collected by centrifugation. The purified tail sheaths were analyzed by SDS‐PAGE and were found to be composed of two proteins (PI and P2) having molecular weights of 52.7 and 41.2 Kd respectively. The location of each of the 4 remaining major structural proteins in the øAa virion remains to be determined.

Original languageEnglish (US)
Pages (from-to)213-218
Number of pages6
JournalOral Microbiology and Immunology
Issue number4
StatePublished - Aug 1990

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Dentistry(all)
  • Microbiology (medical)


  • Actinobacillus actinomycetemcomitans
  • bacteriophage
  • electron microscopy: periodontal disease
  • structural proteins

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