PubMed Health⌕ Search

Biomedical subjects

E C Gotschlich

Publications and source records attributed to E C Gotschlich.

At least 91 records · Page 5Linked to original sources
PubMed1978

Antibody responses of human infants to three doses of group A Neisseria meningitidis polysaccharide vaccine administered at two, four, and six months of age.

Infants were immunized with group A Neisseria meningitidis polysaccharide vaccine at two, four, and six months of age. Two lots of group A vaccine that differed in molecular weight were used; lot no. 1980A was of significantly larger molecular size than lot no. A-7. No significant adverse reactions occurred. The geometric mean concentration of serum antibody to group A N. meningitidis one month after the third dose of lot no. 1980A was 0.89 microgram/ml, nearly twice the concentration induced by lot no. A-7 (0.48 microgram/ml). When the infants were 12 months of age, concentrations of antibody in both groups had declined to similar levels, which were still greater than the mean concentration of antibody in unimmunized children. By 18 months of age, the antibody levels of immunized and unimmunized infants were the same. The three-dose schedule resulted in significantly lower concentrations of antibody than previously studied schedules of two doses given three to four months apart.

Age Factors↗
PubMed1978

Gonococcal color and opacity variants: virulence for chicken embryos.

Previous studies have noted that the prevalence of certain gonococcal colony types is influenced by the physiological state of the human host. Consequently eight different gonococcal strains were passed on clear typing medium, and opaque (Op) and transparent (Tr) variants of heavily pilated (P++) bacteria were selected. P++Op and P++Tr were injected into 11-day-old chicken embryos, and the resulting mortality was determined. In every case the Tr variants were more lethal to the embryos than were the Op variants (P = 0.01). P++Tr were stable in vivo, but chicken embryos injected with P++Op strains developed bacteremia with P++Tr organisms. However, chicken blood was not bactericidal for either colonial variant. These results indicate that transparent pilated bacteria may be more virulent than opaque pilated bacteria and that in vivo selection of transparent forms occurs.

Animals↗
PubMed1978

Prospects for the prevention of bacterial meningitis with polysaccharide vaccines.

MOST SUPPURATIVE INFECTIONS OF THE MENINGES ARE CAUSED BY FIVE BACTERIAL SPECIES: Escherichia coli, Haemophilus influenzae type b, Streptococcus pneumoniae, Neisseria meningitidis, and group B streptococcus. The immune response of adults to pneumococcal capsular polysaccharides has been studied in great detail and their responses to meningococcal and H. influenzae type b capsular polysaccharides are quite similar. Immune responses of adults to E. coli and group B streptococcal antigens are disappointing. The responses of children below the age of 7 years differ both quantitatively and in duration. Early experience shows that useful antibody titres can be achieved with certain antigens but further studies are required. In order to prevent bacterial meningitis by immunization, three vaccine formulations will need to be developed. When epidemic meningococcal disease occurs in a population, the vaccine containing only components of the meningococcus would be applied to a large segment of the population to terminate the epidemic. The second vaccine would contain components of H. influenzae type b, pneumococcus, and the meningococcus and would be administered in the first year of life, and repeated at suitable intervals to maintain life-long immunity. The third vaccine, designed to prevent neonatal meningitis caused by E. coli K1 and group B streptococci, would be administered to women preferably during the third trimester of pregnancy, so that their offspring would inherit sufficient antibodies to protect them during the first 3 months of life.The vaccine against the meningococcus is a reality and has been used extensively during major epidemics, with excellent results. The two vaccines for control of endemic bacterial meningitides do not exist as yet, but the prospects are good.

Adult↗
PubMed1977

Hemagglutination by purified type I Escherichia coli pili.

Many enterobacteria can cause agglutination of erythrocytes, but previous investigations have not proven which components of the bacteria are responsible. We used a strain of Escherichia coli K12 which causes mannose-sensitive hemagglutination (HA) of guinea pig cells. Common pili were purified from these bacteria by shearing them from the bacteria followed by selective precipitation in acid and ammonium sulfate. Isopycnic centrifugation in cesium chloride removed the remaining outer membrane protein contaminants. These pili are pure by electron microscopy and gel electrophoresis. By amino acid analysis, they have a mol wt of 17,099 and consist of 45% nonpolar residues. These purified pili agglutinate guinea pig erythrocytes, a reaction that is inhibited by anti-pili antibodies and by saccharides related in structure to D-mannose. Proteolytic treatment of erythrocytes does not diminish HA but rather increases the pili-induced HA of human cells. Neuraminidase enhances HA and mannosidase slightly diminishes it. It is concluded that purified pili alone cause HA of erythrocytes by binding to mannose-like molecules on the erythrocyte surface. Thus HA by bacterial pili serves as a useful model system for the mechanism of bacterial pili attachment ot cell membranes.

Antibodies, Bacterial↗
PubMed1977

Type I Escherichia coli pili: characterization of binding to monkey kidney cells.

We have demonstrated binding of purified pili from a strain of Escherichia coli to Vero cell monolayers as a model of prokaryotic-eukaryotic cell adherence. Pili bound to the tissue culture in a rapid reaction that did not require enzymatic activation. Attachment occurred optimally at pH 4-5 and could be inhibited by analogues of D-mannose, anti-pili antibodies, or by preincubation of tissue cells with mannose-specific plant lectins. Binding remained after treatment of the monolayer with glycosidases, trypsin, or a protease mixture but was enhanced after neuraminidase treatment. These results indicate that bacterial binding can occur via pili which act like lectins and presumably bind to mannose-containing glycoproteins on mammalian cell surfaces.

Antibodies, Bacterial↗
PubMed1977

Structural studies on the sialic acid polysaccharide antigen of Escherichia coli strain Bos-12.

A polysaccharide, antigenically related to group C meningococcus, has been isolated from Escherichia coli strain Bos-12 (016; K92; NM). Like groups B and C meningococcal polysaccharide, the Bos-12 antigen is a pure polymer of sialic acid. 13C NMR studies on the meningococcal group B and C polysaccharides have indicated that the former consists of sialic acid units linked 2 leads to 8- alpha, whereas the latter contains the sialic acid residues linked 2 leads to 9-alpha (Bhattacharjee, A.K., Jennings, H.J., Kenny, C.P., Martin, A., and Smith, I.C.P. (1975), J. Biol. Chem. 250, 1926). Comparison of natural abundance 13C NMR spectra of the Bos-12 polysaccharide with group B and C meningococcal polysaccharides established that Bos-12 was either (a) an equimolar mixture of 2 leads to 8-alpha linked sialic acid homopolymers or (b) a 2 leads to 8-alpha/2 leads to 9-alpha heteropolymer. These possibilities were distinguished in the following manner. The fact that Bos-12 polysaccharide precipitated with anti-group C serum but not with anti-group B serum would seem to exclude a. Further, chemical studies (periodate oxidation followed by tritiated NaBH4 reduction) gave saccharides with a radioactive-labeling pattern expected for alternating 2 leads to 8-alpha/2 leads to 9-alpha sialic acid linkages. Bos-12 is thus an 2 leads to 8/2 lead to 9-alpha heteropolymer.

Borohydrides↗
PubMed1977

Primary structure of human C-reactive protein.

The complete amino acid sequence of human C-reactive protein has been established. Distant homologies to C3 homology region in the CH2 domain of IgG and to C3a anaphylotoxin have been noted. No homology to other immunoglobulin homology regions or to the same homology region in other heavy chains was observed. The previously reported homologies between rabbit and human C-reactive protein and protein C1t have been extended and strengthened.

Amino Acid Sequence↗
PubMed1977

Cross-antigenicity and immunogenicity between capsular polysaccharides of group C Neisseria meningitidis and of Escherichia coli K92.

Antibodies to capsular polysaccharides of group C Neisseria meningitidis are often found in sera of young adults despite infrequent nasopharyngeal carriage and low rate of attack of N. meningitidis in the United States. Thus, experiments were designed for detection of bacteria cross-reactive with N. meningitidis. Among 3,264 cultures of stool, urine, blood, and cerebrospinal fluid, only 14 strains were found to be cross-reactive; all were Escherichia coli possessing the K92 capsular polysaccharide. The somatic O-antigens were 16, 13, 23, and 73; the flagellar antigens were H4 and 34. All K92 strains of E. coli showed the expected fermentations, were sensitive to common antibiotics, and lacked enteropathogenicity. Antigens of both E. coli K92 and group C N. meningitidis are capsular, acidic polysaccharides composed of sialic acid. The K92 polysaccharide is N- but not O-acetylated, sensitive to neuraminidase, and linked by alpha-2,8- alternating with alpha-2,9-ketosidic bonds. The K92 polysaccharides from all E. coli studied had similar biophysical and immunological properties. Intravenous injection of formalin-treated K92 organisms induced precipitating and bactericidal antibodies to polysaccharides of N. meningitidis. E. coli K92 strains may provide an alternative immunogen for prophylaxis against disease due to group C N. meningitidis in infants and young children.

Adult↗
PubMed1977

Streptococcal M protein: an antiphagocytic molecule assembled on the cell wall.

After extraction with nonionic detergent, type 6 streptococcal M protein was found to be composed of multiple proteins ranging in molecular weight from 35,000 to 6,000 daltons. The antiphagocytic proteins, however, were found to be limited to three species having molecular weights of 28,000, 31,000, and 35,000 daltons. These molecules which removed opsonic antibodies from immune serum could be separated from those proteins that had only type specificity. Pulse chase experiments supported by chemical and immunological data suggest that the smaller, type-specific molecules are used to assemble the larger, antiphagocytic proteins. Type 6 M protein was radialabeled and used in a binding assay for the measurement of opsonic antibodies in human serum. Good correlation was observed between binding and the presence of opsonic antibodies in both systems. However, certain sera did exhibit binding but lacked type-specific opsonic activity. Results of competitive inhibition experiments demonstrated that the nonopsonic serum was deficient in certain antibodies that were present in opsonics serum and that the anitphagocytic molecules contained the sites necessary to bind these antibodies.

Amino Acids↗
PubMed1977

Sialic acid-containing polysaccharides of Neisseria meningitidis and Escherichia coli strain Bos-12: structure and immunology.

A polysaccharide antigenically related to that of group C Neisseria meningitidis was isolated from Escherichia coli strain Bos-12 (O48: K91:NM). Like the polysaccharides of groups B and CN. meningitidis, the Bos-12 antigen was shown to be a pure polymer of sialic acid. The 13C-nuclear magnetic resonance studies of the groups B and C polysaccharides indicated that the former consists of units of sialic acid joined in alpha-2 leads to 8 linkages, whereas the latter contains sialic acid residues linked by alpha-2 leads to 9 glycosidic bonds. Chemical and nuclear magnetic resonance studies of the polysaccharide of E. coli strain Bos-12 established that it is a heteropolymer containing both alpha-2 leads to 8 and alpha-2 leads to 9 linkages. Physical parameters including partial specific volume, reduced viscosity, diffusion and sedimentation coefficients, shape, weight-average molecular weight, and the Stokes radius of the polysaccharides of groups A, B, and C N. meningitidis have been determined. The results indicate that the polysaccharides are highly asymmetric and exist in solution as rigid rods; aggregates are formed by the association of these rods. The polysaccharides appear to have "restricted" length.

Antibodies, Bacterial↗
PubMed1977

Neonatal meningitis due of Escherichia coli K1.

Human neonates are uniquely susceptible to serious infections due to Escherichia coli. Investigation of the serotypes of E. coli isolated from neonates with meningitis revealed that greater than 80% of the isolates possessed the capsular polysaccharide antigen designated K1. Cultures of stool from healthy infants, children, and adults have shown that K1 organisms are commonly found in individuals of all ages. Studies of mother-infant pairs have demonstrated transmission of K1 strains from mother to infant shortly after birth. In the rare infant who develops meningitis due to E. coli K1, serotype analysis frequently reveals that the same organism was isolated from the infant's cerebrospinal fluid and from the stools of both mother and infant. Preliminary investigations of humoral immunity demonstrated an age-related acquisition of antibodies to the capsular polysaccharide of E. coli K1 in healthy infants and children. An animal model was developed in which feeding of E. coli K1 to infant rats resulted in colonization, bacteremia, and meningitis in the animals.

Adult↗
PubMed1977

Iodination of Escherichia coli with chloramine T: selective labeling of the outer membrane lipoprotein.

Iodination of Escherichia coli cells with chloramine T preferentially labels the free and murein-bound forms of the outer membrane lipoprotein. Iodination for 15 s at 15 degrees C labels the two forms of the lipoprotein almost exclusively, whereas iodination for 60 s at 25 degrees C also labels the other major outer membrane proteins. Chloramine T iodination is a rapid, simple technique for labeling the outer membrane lipoprotein.

Arginine↗
PubMed1977

Persistence of antibody following immunization of children with groups A and C meningococcal polysaccharide vaccines.

Persistence of antibody following immunization with groups A and C meningococcal polysaccharides was studied in two groups of children. Cohort 1 (20 children, 2 to 11 years of age) received two doses of A vaccine three years apart; cohort 2 (1,345 children, 6 to 8 years of age) received A or C vaccine initially and the heterologous vaccine one year later. No significant reactions were observed. Geometric mean anti-A concentrations one month after primary and booster immunization in cohort 1 were 8.77 and 13.08 microgram/ml, respectively. Mean anti-A concentration declined 32% one year after booster immunization, but then stabilized. Mean anti-A and anti-C concentrations in cohort 2 were 9.35 and 9.12 microgram/ml, respectively, one month after primary immunization. Mean anti-A concentration declined to 5.54 and 3.62 microgram/ml while anti-C levels fell to 2.35 and 1.47 microgram/ml one and four years after immunization. The proportion of children in cohort 2 with greater than or equal to 2.0 microgram/ml of anti-A and anti-C four years after immunization were 80% and 40%, respectively. An antibody concentration greater than or equal to 2.0 microgram/ml has been associated with protection against meningococcal disease. The results suggest that routine immunization of young infants with group A vaccine may result in long-lasting immunity. The usefulness of the presently available group C vaccine appears to be limited to the control of epidemics.

Antibodies, Bacterial↗
PubMed1976

Protection against group B meningococcal disease. I. Comparison of group-specific and type-specific protection in the chick embryo model.

Protection against group B meningococcal infection was examined using the chick embryo. 12-day-old embryos were challenged intravenously with various meningococcal strains. The chick embryo has an active reticuloendothelial system but lacks functional complement. In this model we found that protection against group B infection was primarily group specific. The group B polysaccharide antibody is an effective opsonin, but is a very poor bactericidal antibody. In contrast, the serotype antibody was bactericidal but only slightly protective in the chick embryo where protection is primarily phagocytic in nature. The group-specific and type-specific antibodies are strongly synergistic. Minute amounts of group B polysaccharide antibody caused a very significant increase in the protective effects of the serotype antibody.

Animals↗
PubMed1976

Streptococcal M protein extracted by nonionic detergent. I. Properties of the antiphagocytic and type-specific molecules.

Group A streptococcal M protein was extracted with nonionic detergent and subjected to a number of physical, chemical, and immunological tests. M protein thus extracted was composed of multiple protein bands, ranging from 35,000 down to 6,000 daltons, all having type-specific precipitating activity. The anti-phagocytic proteins, however, were limited to three molecular species having mol wt of 28,000, 31,000, and 35,000 daltons, and could be separated from those proteins that had only type specificity. Physical studies indicated that these proteins existed as individual asymmetrical molecules which were not aggregated. By radiolabeling M protein on living streptococci, it was determined that these protein bands were found on the streptococcal cell wall in this multiple form. Also, by pulse chase experiments supported by chemical and immunological data, evidence was obtained strongly suggesting that the smaller, type-specific molecules are used to assemble the larger, antiphagocytic proteins.

Amino Acids↗
PubMed1976

The serological classification of Neisseria gonorrhoeae. I. Isolation of the outer membrane complex responsible for serotypic specificity.

Neisseria gonorrhoeae has been subdivided into several classes of serological distinct groups. The serotyping system is based upon the antigenic specificity of a protein serotype antigen. This protein is the major polypeptide of the outer membrane of the gonococcus and accounts for over 60% of that membrane's total protein. The serotype antigen complex was isolated by mild extraction of intact organisms in 200 mM lithium acetate buffer, pH 6.0 with 10 mM EDTA for 2 h at 45 degrees C. The extract was fractionated on Sepharose 6B and partially purified by precipitation at pH 4.2 by addition of 10% (vol/vol) acetic acid. Each serotype antigen has a unique subunit molecular size as determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Preliminary typing of a gonococcal strain may be performed by comparative SDA-PAGE. To date, 16 different serotypes, representing a diverse distribution, have been isolated.

Antibody Specificity↗