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Biomedical subjects

L S Sturman

Publications and source records attributed to L S Sturman.

29 records · Page 2Linked to original sources
PubMed1981

Poliovirus adsorption by 34 minerals and soils.

The adsorption of radiolabeled infectious poliovirus type 2 by 34 well-defined soils and mineral substrates was analyzed in a synthetic freshwater medium containing 1 mM CaCl(2) and 1.25 mM NaHCO(3) at pH 7. In a model system, adsorption of poliovirus by Ottawa sand was rapid and reached equilibrium within 1 h at 4 degrees C. Near saturation, the adsorption could be described by the Langmuir equation; the apparent surface saturation was 2.5 x 10(6) plaque-forming units of poliovirus per mg of Ottawa sand. At low surface coverage, adsorption was described by the Freundlich equation. The soils and minerals used ranged from acidic to basic and from high in organic content to organic free. The available negative surface charge on each substrate was measured by the adsorption of a cationic polyelectrolyte, polydiallyldimethylammonium chloride. Most of the substrates adsorbed more than 95% of the virus. In general, soils, in comparison with minerals, were weak adsorbents. Among the soils, muck and Genesee silt loam were the poorest adsorbents; among the minerals, montmorillonite, glauconite, and bituminous shale were the least effective. The most effective adsorbents were magnetite sand and hematite, which are predominantly oxides of iron. Correlation coefficients for substrate properties and virus adsorption revealed that the elemental composition of the adsorbents had little effect on poliovirus uptake. Substrate surface area and pH, by themselves, were not significantly correlated with poliovirus uptake. A strong negative correlation was found between poliovirus adsorption and both the contents of organic matter and the available negative surface charge on the substrates as determined by their capacities for adsorbing the cationic polyelectrolyte, polydiallyldimethylammonium chloride.

Adsorption↗
PubMed1981

Influence of pH and electrolyte composition on adsorption of poliovirus by soils and minerals.

The pH and the nature an concentration of simple electrolytes influenced the interaction of poliovirus type 2 with three soils, a sand, and a clay mineral. In electrolytes above pH 9 the virus was not adsorbed extensively to the substrates, but below pH 7 almost all virus was bound. For each adsorbent there was a characteristic pH region of transition from strong to weak uptake. Differences between the soils in virus uptake were shown to parallel their pH-dependent mineral. In electrolytes above pH 9 the virus was not adsorbed extensively to the substrates, but below pH 7 almost all virus was bound. For each adsorbent there was a characteristic pH region of transition from strong to weak uptake. Differences between the soils in virus uptake were shown to parallel their pH-dependent mineral. In electrolytes above pH 9 the virus was not adsorbed extensively to the substrates, but below pH 7 almost all virus was bound. For each adsorbent there was a characteristic pH region of transition from strong to weak uptake. Differences between the soils in virus uptake were shown to parallel their pH-dependent charge properties, as determined by whole-particle microelectrophoresis. Only when the pH was close to or above the critical region was uptake increased with electrolyte concentration. The transition region for all substrates was above pH 7.5 the isoelectric point of the virus. Thus, it appears that when both the virus and substrate are highly negative charged, repulsive electrostatic effects may exceed inherent attractive interactions, thereby inhibiting adsorption.

Adsorption↗
PubMed1980

Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid.

The two envelope glycoproteins and the viral nucleocapsid of the coronavirus A59 were isolated by solubilization of the viral membrane with Nonidet P-40 at 4 degrees C followed by sucrose density gradient sedimentation. Isolated E2 consisted of rosettes of peplomers, whereas E1, the membrane glycoprotein, was irregular and amorphous. Under certain conditions significant interactions occurred between components of Nonidet P-40-disrupted virions. Incubation of the Nonidet P-40-disrupted virus at 37 degrees C resulted in formation of a complex between one of the viral glycoproteins, E1, and the viral nucleocapsid. This was caused by a temperature-dependent conformational change in E1, resulting in aggregation of E1 and interaction with the viral RNA in the nucleocapsid. E1 also bound rRNA. The E1-nucleocapsid complexes can be distinguished on sucrose and Renografin density gradients from native viral nucleocapsids. The separation of the membrane glycoprotein E1 from the peplomeric glycoprotein E2 permitted preparation of antisera against these isolated proteins. A model is proposed for the arrangement of the three major structural proteins in the coronavirus A59 virion in relation to the viral envelope and RNA.

Capsid↗
PubMed1972

Enhanced growth of a murine coronavirus in transformed mouse cells.

Plaque formation by A59 virus, a murine coronavirus, was facilitated in AL/N and Balb mouse cells transformed by polyoma virus, simian virus 40, murine sarcoma virus, or mammary tumor virus. In these virus-transformed cells, A59 virus plaques were larger, they appeared earlier, and plaquing efficiencies were higher than in normal, untransformed cells. "Spontaneously" transformed AL/N cells behaved similarly to untransformed cells, whereas "spontaneously" transformed Balb cells resembled virus-transformed cell hosts. Both untransformed and transformed AL/N and Balb cells were permissive hosts for A59 virus. However, multiplication of A59 virus was enhanced at least fivefold in the virus-transformed AL/N cell hosts. Larger differences (100-fold or greater) in A59 virus production were obtained during the first cycle of infection in Balb cells at low multiplicities and in AL/N cells after multiple cycles of virus growth. In virus-transformed and "spontaneously" transformed Balb cells, A59 virus induced extensive syncytia formation.

Animals↗
PubMed1969

Formation of viral ribonucleic acid and virus in cells that are permissive or nonpermissive for murine encephalomyelitis virus (GDVII).

GDVII virus growth in BHK-21 cells, a permissive host for the virus, resembled productive infections with other picornaviruses. Virus yields ranged from 100 to 600 plaque-forming units (PFU)/cell. Virus replication in HeLa cells, a nonpermissive host for GDVII virus, was characterized by virus yields of only 0.1 to 5 PFU/cell. Similar low yields of virus have been obtained from HeLa cells at all multiplicities of input up to 6,000 per cell. The progeny particles from HeLa cells were, like the infecting particles, restricted in the HeLa cell host. Despite the great difference in final yields of virus from BHK-21 and HeLa cells, the times when maximal yields were reached were similar. GDVII virus stock grown in BHK-21 cells was designated HeLa(-). A variant of GDVII virus which is capable of extensive growth in HeLa cells was obtained. This variant, designated HeLa(+) GDVII virus, was passaged serially in HeLa cells. Virus yields of 50 to 150 infective virus particles per cell were obtained from infection of HeLa cells with HeLa(+) GDVII virus. The major species of HeLa(+) virus-specific ribonucleic acid (RNA) produced was single stranded and sedimented with an S value of 35S. The rate of accumulation of HeLa(+) virus-specific RNA in HeLa cell cultures was about four times that of HeLa(-) RNA. The amount of virus-specific HeLa(+) RNA formed in HeLa cells was several-fold greater than that of HeLa(-) RNA. With HeLa(-) parent GDVII virus undergoing productive replication in BHK-21 cells or abortive replication in HeLa cells, the major species of virus-specific RNA produced was single stranded and sedimented with an approximate S value of 35S. The amount of HeLa(-) virus-specific RNA extracted from BHK-21 cells was several-fold greater than the amount obtained from HeLa cells.

Centrifugation, Density Gradient↗