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2.
Nuovi Ann Ig Microbiol ; 38(1-2): 31-4, 1987.
Article in English | MEDLINE | ID: mdl-3504275
4.
Microbiologica ; 7(1): 75-8, 1984 Jan.
Article in English | MEDLINE | ID: mdl-6374384

ABSTRACT

Neuraminidase production by reference strains of various group B streptococci serotypes was investigated before and after serial passages in mouse. The enzyme production was tested in culture filtrates using bovine submaxillary mucin as substrate. Although passages in mouse markedly increased the virulence of all the strains it was not possible to demonstrate a relationship between the increased virulence and the enzyme production.


Subject(s)
Neuraminidase/biosynthesis , Streptococcus agalactiae/pathogenicity , Animals , Mice , Mice, Inbred Strains , N-Acetylneuraminic Acid , Neuraminidase/metabolism , Peritoneal Cavity/microbiology , Sialic Acids/biosynthesis , Streptococcus agalactiae/enzymology , Virulence
5.
Boll Ist Sieroter Milan ; 60(4): 284-7, 1981.
Article in English | MEDLINE | ID: mdl-7326103

ABSTRACT

A total of 100 strains of Proteus, clinically isolated, were tested for sensitivity to ovotransferrin and CrCl3. Only a minority of the tested strains were not capable of growing in the presence of these iron chelating substances. Significant differences in the resistance among the four species of Proteus were noticeable only by addition to the culture medium of CrCl3 5 mM. The fact that sensitive strains were capable of growing after addition of citrate to culture medium containing ovotransferrin or CrCl3 suggests the presence in the genus Proteus of a citrate-dependent iron transport system.


Subject(s)
Chlorides , Chromium Compounds , Conalbumin/pharmacology , Egg Proteins/pharmacology , Proteus/drug effects , Chromium/pharmacology , Citrates/metabolism , Citric Acid , Drug Resistance, Microbial , Proteus/growth & development
7.
Acta Virol ; 24(5): 311-6, 1980 Sep.
Article in English | MEDLINE | ID: mdl-6108058

ABSTRACT

The haemagglutination-inhibiting activity of human serum towards Sindbis virus is linked to very low and low density lipoprotein classes, in particular to their lipid component. To investigate the specific role played in this inhibition by carbohydrates contained in the molecule, inhibitor separation was carried out by Concanavalin A-Sepharose affinity chromatography. A different behaviour among the inhibiting molecules in relation to the carbohydrate content was observed. The importance of mannose for the biological activity of the inhibitor is discussed.


Subject(s)
Hemagglutination, Viral/drug effects , Lipoproteins, LDL/pharmacology , Lipoproteins, VLDL/pharmacology , Sindbis Virus/physiology , Carbohydrates/analysis , Chromatography, Affinity , Humans , Lipoproteins, LDL/analysis , Lipoproteins, LDL/isolation & purification , Lipoproteins, VLDL/analysis , Lipoproteins, VLDL/isolation & purification
8.
J Clin Microbiol ; 11(5): 445-7, 1980 May.
Article in English | MEDLINE | ID: mdl-7381007

ABSTRACT

A total of 150 strains of staphylococci, clinically isolated, were tested for sensitivity to ovotransferrin (conalbumin). Among these, all the 50 coagulase-positive, mannitol-positive, and deoxyribonuclease-positive staphylococci appeared to be resistant to conalbumin, i.e., capable of growing in the presence of this transferrin. Among the other 100 strains, which were not classified as S. aureus, some appeared to be resistant and some were sensitive. The different behavior toward conalbumin is related to varying degrees of efficiency of the bacterial iron transport systems and, to test this, a simple method can be used, based on the addition of CrCl3 to the culture medium. The precipitation of iron produced by chromium salts has an effect on the growth of staphylococci similar to that produced by conalbumin and reveals the differences in the iron transport systems which occur in the genus Staphylococcus.


Subject(s)
Chromium/pharmacology , Conalbumin/pharmacology , Egg Proteins/pharmacology , Staphylococcus aureus/pathogenicity , Staphylococcus/pathogenicity , Biological Transport , Iron/metabolism , Staphylococcus/metabolism , Staphylococcus aureus/drug effects , Staphylococcus aureus/metabolism
9.
Boll Ist Sieroter Milan ; 58(5): 365-70, 1979 Nov 30.
Article in English | MEDLINE | ID: mdl-95432

ABSTRACT

Research was carried out in order to verify if some components of human serum, which are capable of inhibiting the hemagglutination by Sendai virus, are active even towards the hemolysis by the same virus. It was ascertained that both orosomucoid and low-density lipoproteins obtained by floatation had no action on the hemolysis by Sendai virus while lipoproteins precipitated with dextrane sulphate showed a certain inhibiting effect. This action however is not due to lipoproteins but is probably related to some substances used in the method of precipitation.


Subject(s)
Antibodies, Viral , Hemolysis , Parainfluenza Virus 1, Human , Chemical Precipitation , Dextrans/pharmacology , Female , Hemagglutination Tests , Humans , Lipoproteins, LDL , Male , Orosomucoid , Protamines/pharmacology
14.
Boll Ist Sieroter Milan ; 57(6): 700-6, 1979 Jan 31.
Article in English | MEDLINE | ID: mdl-233295

ABSTRACT

Non-antibody hemagglutination-inhibiting activity of human serum is due, at least partially, to a glycoprotein inhibitor. This inhibitor was obtained from the whole serum or the fraction VI (Cohn) by means of methods of purification generally used for the preparation of the orosomucoid and was identified more precisely with an acid alpha 1-glycoprotein.


Subject(s)
Glycoproteins/pharmacology , Parainfluenza Virus 1, Human/immunology , Animals , Blood Proteins , Chickens , Electrophoresis, Polyacrylamide Gel , Female , Hemagglutination Inhibition Tests , Humans , Male , Orosomucoid/pharmacology , Serum Albumin
16.
Boll Ist Sieroter Milan ; 57(1): 54-9, 1978 Mar 31.
Article in Italian | MEDLINE | ID: mdl-207291

ABSTRACT

An investigation has been carried out in order to ascertain the effect of the presence of complement on the HI antibodies of the IgM class obtained in rabbit against Sendai virus. Contrary to the results obtained by some AA. with other viruses, in this case the presence of complement in the form of fresh guinea-pig serum has not modified the HI titre. It has however been demonstrated that in the guinea-pig serum an inhibitor is present, which is active towards Sendai virus and can be identified as a 19S alpha-globulin.


Subject(s)
Antibodies, Viral , Complement System Proteins , Immunoglobulin M , Parainfluenza Virus 1, Human/immunology , Animals , Antibodies, Viral/analysis , Guinea Pigs , Hemagglutination Inhibition Tests , Immunoglobulin M/analysis , Rabbits
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