Abstract
The bacteriolytic activity of normal human serum on a rough strain of E. coli has been studied by a turbidimetric method. Bacteriolysis was found to be markedly dependent on ionic strength and pH, with optima at µ = 0.06 and pH 8.3–8.5, respectively. The method of cultivating the cells also influenced the rapidity of lysis. Lysis was temperature-dependent and was exhibited by all samples of human serum tested. Microscopically, organisms incubated with serum were observed to swell, loose their rod shape and eventually burst, leaving remnants of the cell membrane in suspension. Sphaeroplasts were obtained by brief exposure of cells to serum followed by dilution into 5 per cent sucrose. The bacteriolytic reaction was shown to require complement. No definite requirement for properdin or specific antibody in this system could be demonstrated by the absorption of serum with zymosan and with homologous cells respectively. The latter procedure was found to reduce bacteriolytic activity by removal of serum lysozyme. Absorption of serum with bentonite also led to loss of bacteriolytic activity which could be restored with lysozyme. The organism was not lysed by lysozyme alone, but lysis occurred with lysozyme + EDTA in tris buffer. The possibility of complement acting independently of antibody or properdin, in certain instances, is discussed in relation to bacterial cell wall structure. Data are presented supporting the hypothesis that the "substrate" of complement in cell membranes is a lipid or lipoprotein.
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- AUSTEN K. F. The differentiation of the chloroform, peptone and antigen-antibody inducible esterase activities of human serum from plasmin. Immunology. 1960 Apr;3:152–173. [PMC free article] [PubMed] [Google Scholar]
- BECKER E. L. Concerning the mechanism of complement action. IV. The properties of activated first component of guinea pig complement. J Immunol. 1959 Jan;82(1):43–51. [PubMed] [Google Scholar]
- COLOBERT L. Etude de la lyse de salmonelles pathogènes provoquée par le lysozyme, après délipidation partielle de la paroi externe. Ann Inst Pasteur (Paris) 1958 Aug;95(2):156–167. [PubMed] [Google Scholar]
- DAVIS B. D., MINGIOLI E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol. 1950 Jul;60(1):17–28. doi: 10.1128/jb.60.1.17-28.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LEVINE L., WASSERMAN E., MILLS S. Complement fixation and ionic strength. J Immunol. 1961 Jun;86:675–680. [PubMed] [Google Scholar]
- MANDELSTAM J. Isolation of lysozyme-soluble mucopeptides from the cells wall of Escherichia coli. Nature. 1961 Mar 11;189:855–856. doi: 10.1038/189855a0. [DOI] [PubMed] [Google Scholar]
- MARCUS S., ESPLIN D. W., DONALDSON D. M. Lack of bactericidal effect of mouse serum on a number of common microorganisms. Science. 1954 Jun 18;119(3103):877–877. doi: 10.1126/science.119.3103.877. [DOI] [PubMed] [Google Scholar]
- MICHAEL J. G., BRAUN W. Serum spheroplasts of Shigella dysenteriae. Proc Soc Exp Biol Med. 1959 Feb;100(2):422–425. doi: 10.3181/00379727-100-24649. [DOI] [PubMed] [Google Scholar]
- MICHAEL J. G., LANDY M. Endotoxic properties of gramnegative bacteria and their susceptibility to the lethal effect of normal serum. J Infect Dis. 1961 Jan-Feb;108:90–94. doi: 10.1093/infdis/108.1.90. [DOI] [PubMed] [Google Scholar]
- MYRVIK Q. N., WEISER R. S. Studies on antibacterial factors in mammalian tissues and fluids. I. A serum bactericidin for Bacillus subtilis. J Immunol. 1955 Jan;74(1):9–16. [PubMed] [Google Scholar]
- Mayer M. M., Osler A. G., Bier O. G., Heidelberger M. THE ACTIVATING EFFECT OF MAGNESIUM AND OTHER CATIONS ON THE HEMOLYTIC FUNCTION OF COMPLEMENT. J Exp Med. 1946 Nov 30;84(6):535–548. doi: 10.1084/jem.84.6.535. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McGHEE R. B. Presence of complement in serum of the mouse. Proc Soc Exp Biol Med. 1952 Jul;80(3):419–420. doi: 10.3181/00379727-80-19642. [DOI] [PubMed] [Google Scholar]
- NOLLER E. C., HARTSELL S. E. Bacteriolysis of Enterobacteriaceae. I. Lysis by four lytic systems utilizing lysozyme. J Bacteriol. 1961 Mar;81:482–491. doi: 10.1128/jb.81.3.482-491.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NOLLER E. C., HARTSELL S. E. Bacteriolysis of Enterobacteriaceae. II. Pre- and co-lytic treatments potentiating the action of lysozyme. J Bacteriol. 1961 Mar;81:492–499. doi: 10.1128/jb.81.3.492-499.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- REPASKE R. Lysis of gram-negative bacteria by lysozyme. Biochim Biophys Acta. 1956 Oct;22(1):189–191. doi: 10.1016/0006-3002(56)90240-2. [DOI] [PubMed] [Google Scholar]
- REPASKE R. Lysis of gram-negative organisms and the role of versene. Biochim Biophys Acta. 1958 Nov;30(2):225–232. doi: 10.1016/0006-3002(58)90044-1. [DOI] [PubMed] [Google Scholar]
- WARDLAW A. C., PILLEMER L. The properdin system and immunity. V. The bactericidal activity of the properdin system. J Exp Med. 1956 May 1;103(5):553–575. doi: 10.1084/jem.103.5.553. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WARREN G. H., GRAY J., YURCHENCO J. A. Effect of polymyxin on the lysis of Neisseria catarrhalis by lysozyme. J Bacteriol. 1957 Dec;74(6):788–793. doi: 10.1128/jb.74.6.788-793.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
