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J C Hierholzer

Publications and source records attributed to J C Hierholzer.

At least 109 records · Page 6Linked to original sources

New human adenovirus isolated from a renal transplant recipient: description and characterization of candiate adenovirus type 34.

An antigenically distinct adenovirus is described which was isolated in March 1972 from the urine of a 17-year-old Caucasian male who was experiencing fever after receiving a kidney transplant from a cadaver in February. The adenovirus could not be isolated in April from a pharyngeal swab which yielded cytomegalovirus. Complement-fixation, hemagglutination-inhibition, and/or serum-neutralization tests on sequential serum specimens from the patient confirmed that the adenovirus infection occurred during March and showed that infections with cytomegalovirus and respiratory syncytial virus also occurred during late March and April. The patient's persistent fever, for which other causes could not be found, may have been associated with one or more of these infections. Upper respiratory symptoms and lung involvement were not found during this period. Mild liver dysfunction during this time could not be clearly related to adenovirus infection because of the presence of multiple other causes. The adenovirus may have been latent in the donor kidney and become active in the new host as a consequence of immunological impairment. The adenovirus, purified by terminal dilution and plaque procedures, has antigenic, morphological, biophysical, host susceptibility, and hemagglutinating properties characteristic of adenovirus group IA. Buoyant densities in CsCl are 1.340 g/ml for the virion, 1.304 g/ml for the group CF antigen (hexon), 1.295 g/ml for the major soluble complete hemagglutinin (dodecon), and 1.206 g/ml for the minor soluble complete hemagglutinin (tentatively, fiber dimer). The virus does not cross-react in reciprocal hemagglutination-inhibition and serum-neutralization tests with antisera to adenovirus types 1 to 33. We propose this virus as candidate adenovirus type 34 (Compton).

Adenoviridae↗

Physicochemical and serological characteristics of respiratory virus fluorescein-isothiocyanate conjugates for fluorescent-antibody diagnosis.

Fluorescein-isothiocyanate (FITC) conjugates were prepared by improved methods from standard reference antisera to influenza A and B, mumps, parainfluenza 1, 2, 3, and 4, herpesvirus, respiratory syncytial virus, and adenovirus hexon. The antisera, prepared in a variety of animals, were fractionated three times with selected optimal concentrations of ammonium sulfate and yielded gamma globulins of adequate purity for conjugation with FITC. Conjugates containing optimal fluorescein-to-protein ratios of between 5 and 10 were produced in 2 h by dialysis labeling. Serological titers of each antiserum and conjugate were determined by complement fixation, hemagglutination-inhibition, serum neutralization, and indirect hemagglutination tests where appropriate. When corrected for dilution, the serological titers of the FITC conjugates were identical to those of the starting antisera. The fluorescent-antibody staining titers correlated well with one of the serological parameters of the original serum. The conjugates stained homologous antigens specifically and were free of nonspecific staining at the working dilution. Undesired staining of host cells which was a problem with some of the conjugates produced from sera containing cellular antibodies was removed by absorption with packed cells. These physicochemical and serological findings were then used as a guide in preparing high quality reagents for fluorescent-antibody identification of respiratory viruses.

Adenoviridae↗

Purification and properties of a glycoprotein acid phosphatase from Candida albicans.

An acid phosphomonoesterase was purified 87-fold with a 4% recovery from disintegrated cells of Candida albicans by four stages of column chromatography. The purified enzyme was homogeneous by ultracentrifugal, electrophoretic, and immunological analyses. The fully corrected sedimentation coefficient, s(20,w), was calculated to be 5.51s. Molecular weight estimated from ultracentrifugal data was 124.3 x 10(3), from gel chromatography was 115 x 10(3), and from acrylamide gel electrophoretic data was 131 x 10(3). Buoyant density in sucrose was 1.15 g/cm(3). The enzyme was a mannoprotein with a hexose to protein ratio of 7: 1. The Michaelis constant of the enzyme was 3.3 x 10(-4) M for p-nitrophenyl phosphate as substrate, and the pH optimum was 4.5. The enzyme was competitively inhibited by inorganic phosphate (K(i) = 10(-4) M) and by arsenate (K(i) = 0.5 x 10(-4) M). A wide range of inorganic cations and anions did not affect enzyme activity, but Hg(2+), Cd(2+), and Cu(2+) were inhibitory. F(-) was also inhibitory at low concentrations, but the effect was reversed at higher concentrations. Phosphatase activity was completely destroyed by exposure of the enzyme to 70 C for 12 min, but was destroyed only slowly by proteolytic hydrolysis. The purified glycoprotein enzyme gave a line of identity with the "b" antigen of crude C. albicans homogenates in immunodiffusion and immunoelectrophoresis tests with sera from rabbits inoculated with intact C. albicans cells and from humans with proven candidiasis. Preliminary evidence suggests that the mannan and not the protein portion of the enzyme molecule is responsible for this antigenicity.

Acid Phosphatase↗

Comparison of immunization methods for producing reference adenovirus antisera in horses.

Horses were immunized by a variety of inoculation procedures designed to determine the most efficient method of producing antisera to adenovirus types 25 to 31. The procedures evaluated included immunization by (i) direct intravenous (iv) injection, (ii) iv infusion, (iii) intramuscular (im) injection of virus with and without Freund's incomplete adjuvant, (iv) combined iv and im injections, and (v) combined iv infusion and im injection. The im schedule (no. 3) was superior to the others in terms of immunizing antigen and time required, and hemagglutination-inhibition (HI) and serum-neutralizing (SN) antibody levels produced. HI and SN tests performed with sera before and after heating at 56 C for 30 min showed that heat-inactivation was not necessary for tests with equine antisera.

Adenoviridae↗