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HSV-1 multiplication rates have been shown to vary in different tissues and the rate of multiplication may correlate with susceptibility to antiviral chemotherapy. Herpetic stromal keratitis is a necrotizing condition refractive to antiviral therapy and this lack of antiviral efficacy in stromal disease may be the result of very low rates of viral replication in the corneal stromal keratocytes. In this study, we investigated the efficacy of antiviral drugs in an in vitro system in which the virus multiplication rate is slow. In this system, the reduced rate of virus multiplication is achieved by a reduction in the incubation temperature. Vero cells were infected at one of several multiplicities of infection with McKrae strain HSV-1 and incubated for 24, 48, or 72 h at 26 or 36.5 degrees C in the presence or absence of trifluridine (50 micrograms/ml) or acyclovir (20 micrograms/ml). Both drugs suppressed viral replication at 36.5 degrees C. However, under some specific sets of conditions, trifluridine was not effective in suppressing viral replication in cells incubated at 26 degrees C. At this temperature, viral replication and cell metabolism are slowed to a pace which may be similar to that which occurs in corneal stromal keratocytes in vivo. Acyclovir significantly reduced HSV-1 replication under all conditions at 26 degrees C, indicating that the antiviral activity of this compound is effective in cells whose metabolic rate is slow and in which viral replication is taking place slowly.

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In this study cyst walls of Hartmannella glebae were isolated and quantitatively analyzed. They were fractionated into alkali-insoluble and alkali-soluble fractions. The alkali-insoluble fraction appeared to be cellulose which represented 4.2% of the total weight of the wall. The major component of the alkali-soluble fraction consisted of proteins (64.7%). It also contained a glucose polymer (probably a precursor of cellulose) and lipids. The amino acid composition of the wall was also determined.

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Two bacteriolytic enzymes were produced when Hartmanella glebae was grown in the presence of both Enterobacter aerogenes and Alcaligenes faecalis. The identification of enzyme I as N-acetylmuramidase was reported earlier. Enzyme II was purified by gel filtration on a Bio-Gel A column. A recovery of 68.76% with 72.3-fold purification was obtained. It was found that 5 and 10 mM MgCl2 significantly increased the bacteriolytic activity. It is a basic protein. The cell walls of Micrococcus lysodeikticus were lysed by the enzyme, and the products of digestion were purified by Amberlite CG-120 and Sephadex G-15 chromatography to facilitate the detection of amino sugars. After reduction of the oligosaccharides with sodium borohydride and acid hydrolysis, the amino sugars were identified by paper chromatography. It was found that enzyme II cleaved the glycosidic bond between N-acetylmuramic and and N-acetylglucosamine of the peptidoglycan moiety of the cell walls. Thus, the enzyme was identified as endo-beta-N-acetylmuramidase.

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A soil amoeba (Hartmannella glebae), when grown in conjunction with Enterobacter aerogenes and Alcaligenes faecalis, produced two enzymes. Enzyme I was purified by gel filtration on Sephadex G-100 and chromatography on diethylaminoethyl-cellulose. It is a basic protein. The analysis of the enzymic digest of the cell walls of Micrococcus lysodeikticus after reduction and acid hydrolysis showed that the enzyme cleaved the glycosidic bond between acetylmuramic acid and acetylglucosamine of the peptidoglycan moiety of the cell walls. The enzyme is identified as endo-beta-N-acetylmuramidase.

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A soil amoeba, Hartmannella glebae, could grow on a variety of gram-positive and gram-negative bacteria, although the rate of growth was faster in the presence of gram-negative bacteria. The amoeba, however, could not use yeasts, molds, or a green alga as a nutritional source. The extract prepared from amoebae grown in the presence of Aerobacter aerogenes and Alcaligenes faecalis could lyse intact cells and cell walls of many gram-positive bacteria at different rates. The spectrum of lytic activity was similar to that of egg-white lysozyme, with the exception that several species and strains of Bacillus, Micrococcus, and Staphylococcus were resistant to lysozyme and susceptible to the extract. The gram-negative bacteria tested were resistant.

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