Fibrous dysplasia of the middle turbinate with primary hyperparathyroidism.
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Endoscopy↗
Biomedical subjects
M H Klein
Publications and source records attributed to M H Klein.
Effect of lipid modification on the physicochemical, structural, antigenic and immunoprotective properties of Haemophilus influenzae outer membrane protein P6.
The outer membrane lipoprotein, P6 of Haemophilus influenzae was studied to determine the importance of the native palmitoyl moiety on its physicochemical and immunological properties. A recombinant P6 (rP6) molecule devoid of lipidation signal sequence was expressed in Escherichia coli and its properties were compared to those of the palmitylated protein purified from H. influenzae. The isoelectric point of rP6 was more acidic than that of the native protein and also exhibited less secondary structure than P6 as judged by circular dichroism. However, both forms of P6 induced identical P6-specific antibody titers in guinea pigs when Freund's adjuvant was used. These antisera reacted with a panel of overlapping P6 peptides in a comparable manner and in addition, rabbit antisera raised against the P6 peptides reacted equally well with P6 and rP6. Furthermore, all human convalescent sera tested exhibited similar anti-P6 and anti-rP6 antibody titers. However, rP6 was less immunogenic than P6 when administered either without adjuvant or in alum and when tested in competitive inhibition studies with anti-P6 antibodies, was a less effective inhibitor than native P6, suggesting a diminution in some of the antigenic activity of rP6. In spite of these differences, rP6 was capable of eliciting a protective antibody response against live H. influenzae type b challenge in a modified infant rat model of bacteremia. These findings demonstrate that the non-fatty acylated rP6 could possibily be substituted for native P6 in a vaccine against H. influenzae.
Amino Acid Sequence↗
Length of maternity leave and quality of mother-infant interactions.
The aim of this study was to assess the association between the length of maternity leave and the quality of mother-infant interactions; 198 employed mothers of 4-month-old infants were interviewed and videotaped in their homes during a feeding time. Hierarchical multiple regression analyses indicated a direct association between shorter length of leave and more negative affect and behavior in maternal interactions with their infants. Infant and mother stressor/protective variables added significantly in predicting the quality of the mother-infant relationship. There were also significant interaction effects between the length of leave and these variables. Mothers who either reported more depressive symptoms or who perceived their infant as having a more difficult temperament and who had shorter leaves, compared with mothers who had longer leaves, were observed to express less positive affect, sensitivity, and responsiveness in interactions with their infants. The public policy implications of the relation between length of maternity leave, maternal and infant individual differences, and the quality of mother-infant interactions are discussed.
Adult↗
The major outer membrane protein, CD, extracted from Moraxella (Branhamella) catarrhalis is a potential vaccine antigen that induces bactericidal antibodies.
The major outer membrane protein of Moraxella (Branhamella) catarrhalis, CD, was detergent-extracted from the bacterial cell wall and purified to homogeneity in high yields by a simple process. The purified protein appeared to exhibit immunogenic properties similar to those of native CD exposed on the surface of the bacterium. Antibodies to CD raised in mice specifically bound to intact B. catarrhalis, as determined by flow cytometry analysis. The IgG subclass distributions of anti-CD antibodies in sera from mice immunized with purified CD or with B. catarrhalis were also similar. CD was found to be antigenically conserved among a panel of B. catarrhalis isolates, as demonstrated by the consistent reactivities of mouse anti-CD antisera with a common 60 kDa protein on immunoblots. Furthermore, convalescent sera collected from patients with otitis media due to B. catarrhalis infection were found to be reactive with the CD protein by immunoblotting. Finally, the purified protein induced antibodies in guinea pigs and mice that exhibited in vitro bactericidal activity against the pathogen. Therefore, the native CD outer membrane protein represents a potentially useful antigen for inclusion in a vaccine against B. catarrhalis.
Amino Acid Sequence↗
Outer membrane protein D15 is conserved among Haemophilus influenzae species and may represent a universal protective antigen against invasive disease.
We have cloned and sequenced the d15 gene from two strains of Haemophilus influenzae type b (Hib) and two strains of nontypeable H. influenzae (NTHI). The nucleotide and deduced protein sequences of d15 are highly conserved, with only a small variable region identified near the carboxyl terminus of the protein. Analysis of upstream sequences revealed that the H. influenzae d15 gene may be part of a large potential operon of closely spaced open reading frames, including one with significant homology to the Escherichia coli cds gene encoding CDP-diglyceride synthetase. Southern blot analysis demonstrated that the d15 gene is also present in H. influenzae types a, c, d, e, and f and in Haemophilus parainfluenzae. A recombinant D15 (rD15) protein was expressed in good quantity in E. coli from the inducible T7 promoter, and monospecific anti-rD15 antibodies were raised. Immunoblot analysis of H. influenzae serotypes a, b, c, d, e, and f, NTHI, and H. parainfluenzae lysates revealed that they all expressed a cross-reactive D15-like protein. Purified rD15 was found to be highly immunogenic in mice, guinea pigs, and rabbits, and passive transfer of anti-rD15 antibodies protected infant rats from challenge with H. influenzae type b or type a in infant rat models of bacteremia. Thus, D15 is a highly conserved antigen that is protective in animal models and it may be a useful component of a universal subunit vaccine against Haemophilus infection and disease.
Amino Acid Sequence↗
Sequences of the genes encoding the A, B and C subunits of the Haemophilus influenzae dimethylsulfoxide reductase complex.
The genes (dms) encoding the dimethylsulfoxide reductase protein complex have been cloned and sequenced from Haemophilus influenzae (Hi) type b (Hib) strain Eagan. The Hib dms genes are arranged as an operon whose genomic organization is similar to that of the Escherichia coli (Ec) dmsABC operon. The deduced Hib DmsA, and DmsB and DmsC amino-acid sequences are highly homologous to their Ec counterparts and nearly identical to the recently published sequences of the Hi type-d strain Rd Dms proteins. Hi dimethylsulfoxide reductase appears to be a new member of the superfamily of oxidoreductase enzymes.
Base Sequence↗
Relationship of social perceptions and self-concept in bulimia nervosa.
Although numerous studies have examined the families of bulimic individuals, none have explicitly addressed how family factors relate to self-concept among patients with bulimia. This study used L. Benjamin's' structural analysis of social behavior (1974) rating scales to assess how perceptions of parental relationships relate to self-concept. The results indicate that female patients with bulimia perceive both parents as hostilely disengaged. Furthermore, the self-concepts of patients with bulimia were significantly associated with perceptions of paternal attack/friendliness, which differentiated them from control participants. The results are discussed in terms of the possible relations between family factors and self-concept in bulimia.
Adolescent↗
Cloning and expression of the Haemophilus influenzae transferrin receptor genes.
The genomic transferrin receptor genes (tbpA and tbpB) from two strains of Haemophilus influenzae type b (Hib) and two strains of non-typable H. influenzae (NTHi) have been cloned and sequenced. The deduced protein sequences of the H. influenzae tbpA genes were 95-100% conserved and those of the tbpB genes were 66-100% conserved. The tbpB gene from one strain of NTHi was found to encode a truncated Tbp2 protein. The tbpB genes from four additional NTHi strains were amplified by the polymerase chain reaction (PCR) utilizing primers derived from the conserved N-terminal sequences of Tbp1 and Tbp2 and were found to encode full-length proteins. Although several bacterial species express transferrin receptors, when the Tbp1 and Tbp2 sequences from different organisms were compared, there was only limited homology. Recombinant Tbp1 and Tbp2 proteins were expressed from Escherichia coli and antisera were raised to the purified proteins. There was significant antigenic conservation of both Tbp1 and Tbp2 amongst H. influenzae strains, as determined by Western blot analysis. In a passive model of bacteraemia, infant rats were protected from challenge with Hib after transfer of anti-rTbp2 antiserum, but not after anti-rTbp1 antiserum.
Amino Acid Sequence↗
Advantages of autologous fascia versus synthetic patch abdominal reconstruction in experimental animal defects.
Although prosthetic patches (i.e., expanded polytetrafluoroethylene) are commonly used to repair abdominal fascial defects, autologous tissue is preferred in the presence of wound contamination. This study was undertaken to discover (1) whether fascial grafts are revascularized and incorporated as living tissue, and (2) whether fascial grafts are more resistant to bacterial contamination than prosthetic patches. In the first experiment, 18 New Zealand White rabbits underwent full-thickness resection of the central abdominal wall preserving only panniculus carnosus and skin. Six control animals had only skin repaired, and all developed large ventral hernias. Twelve animals had the defect repaired with thoracodorsal fascia patches. At 3- and 6-week intervals, no hernias were present and all patches were incorporated with minimal contraction. Fluorescein angiography verified revascularization from the surrounding abdominal wall. Next, 36 rabbits underwent similar resection followed by repair with either autologous fascia (n=18) or expanded polytetrafluoroethylene (n=17). Six rabbits of each repair group were inoculated with 10(4) Staphylococcus aureus and twelve rabbits with each repair were inoculated with 10(9) S. aureus. All rabbits receiving 10(4) S. aureus were infection-free survivors. Seven of the twelve expanded polytetrafluoroethylene-repaired animals receiving 10(9) S. aureus developed necrotizing wound infections and died. Only 2 of 12 rabbits with autologous fascia repairs died from wound sepsis and 1 died of diarrhea with a healed wound. Differences in wound infection rates achieved statistical significance, whereas survival differences approached significance (Fisher's exact test), suggesting that revascularized fascial grafts may be more resistant to bacterial contamination than expanded polytetrafluoroethylene patches at this concentration (10(9) S. aureus).
Abdominal Muscles↗
Bilateral elastofibroma: a case report and review of the literature.
Elastofibroma, or elastofibroma dorsi as it was first described, is an uncommon tumor-like process that characteristically appears as an ill-defined mass in the infrascapular region of elderly patients. This lesion can occur bilaterally and may appear asynchronously. The occurrence of elastofibroma in other anatomic sites has been reported, although with much less frequency. Elastofibromas display typical diagnostic histologic, cytologic, and electron microscopic features. The use of magnetic resonance imaging can lead to a presumptive diagnosis in elderly individuals with suprascapular lesions. It is important to differentiate this lesion from other soft-tissue lesions, such as sarcomas and desmoid tumors. This study presents a case of bilateral elastofibromas in a 72-year-old man and a review of the literature.
Aged↗
Poliovirus hybrids expressing neutralization epitopes from variable domains I and IV of the major outer membrane protein of Chlamydia trachomatis elicit broadly cross-reactive C. trachomatis-neutralizing antibodies.
Trachoma and sexually transmitted diseases caused by Chlamydia trachomatis are major health problems worldwide. Epitopes from the variable domains of the major outer membrane protein are candidates for vaccine development. We have constructed hybrid polioviruses expressing sequences from major outer membrane protein variable domains I and IV. Antisera to the hybrids could, in combination, strongly neutralize 8 of the 12 C. trachomatis serovars most commonly associated with oculogenital infections and weakly neutralize the others.
Amino Acid Sequence↗
Gene assembly-aided mutagenesis (GAAM).
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DNA Primers↗
Residue at position 331 in the IgG1 and IgG4 CH2 domains contributes to their differential ability to bind and activate complement.
A conserved proline residue is found at position 331 in the CH2 domains of human IgG subclasses which fix complement. This residue is replaced by a serine in IgG4 which is inactive. To determine the role of residue 331 in the differential ability of human IgGs to activate the complement cascade, a pair of genetically engineered anti-dinitrophenol IgG1 and IgG4 antibodies with reciprocal mutations at position 331 were tested for their hemolytic activity as well as for their ability to bind C1q, activate C1 and cleave C4. The IgG1 Ser331 mutant was virtually unable to mediate the lysis of trinitrobenzene-sulfonic acid-derivatized sheep red blood cells as a result of a marked defect in C1q binding activity. In contrast, the substitution of Pro for Ser331 in IgG4 bestowed partial hemolytic activity (40%) to the IgG4 Pro331 variant. Under low ionic strength conditions, this mutant was found to be approximately 50 and 75% as active as wild-type IgG1 in the C1q binding and C4b deposition assays, respectively. These results indicate that residue Pro331, which folds into close proximity to a previously identified C1q binding motif (Duncan, A. R., and Winter, G. (1988) Nature 332, 738-740), contributes to the architecture of the IgG1 C1q binding site and that its replacement by a serine residue in IgG4 is largely responsible for the functional inactivity of this isotype.
Amino Acid Sequence↗
The crystal structure of pertussis toxin.
BACKGROUND: Pertussis toxin is an exotoxin of the A-B class produced by Bordetella pertussis. The holotoxin comprises 952 residues forming six subunits (five different sequences, S1-S5). It plays an important role in the development of protective immunity to whooping cough, and is an essential component of new acellular vaccines. It is also widely used as a biochemical tool to ADP-ribosylate GTP-binding proteins in the study of signal transduction. RESULTS: The crystal structure of pertussis toxin has been determined at 2.9 A resolution. The catalytic A-subunit (S1) shares structural homology with other ADP-ribosylating bacterial toxins, although differences in the carboxy-terminal portion explain its unique activation mechanism. Despite its heterogeneous subunit composition, the structure of the cell-binding B-oligomer (S2, S3, two copies of S4, and S5) resembles the symmetrical B-pentamers of the cholera toxin and Shiga toxin families, but it interacts differently with the A-subunit. The structural similarity is all the more surprising given that there is almost no sequence homology between B-subunits of the different toxins. Two peripheral domains that are unique to the pertussis toxin B-oligomer show unexpected structural homology with a calcium-dependent eukaryotic lectin, and reveal possible receptor-binding sites. CONCLUSION: The structure provides insight into the pathogenic mechanisms of pertussis toxin and the evolution of bacterial toxins. Knowledge of the tertiary structure of the active site forms a rational basis for elimination of catalytic activity in recombinant molecules for vaccine use.
Amino Acid Sequence↗
Five-year outcome from eating disorders: relevance of personality disorders.
In order to assess the relationship of personality disorder and eating disorder outcome 30 eating disordered patients were followed up 4-5 years after taking part in a study examining the prevalence of personality disorders in eating disordered individuals. Subjects with personality disorders did not differ from those without personality disorders in the amount of symptomatic change over time, although their psychopathology generally remained more severe. The relationship of personality disorder and clinical outcome ratings varied depending on the personality measure. SCID-II personality disorder diagnoses were not significantly associated with outcome ratings, but were related to a greater likelihood to be hospitalized and treated with psychotropic medications. Results with a new personality measure, the Wisconsin Personality Inventory, did display an association between personality disturbance and eating disorder outcome ratings and also suggested that borderline personality was a significant predictor of outcome.
Adolescent↗
A prototype recombinant vaccine against respiratory syncytial virus and parainfluenza virus type 3.
We have produced a genetically-engineered chimeric protein composed of the external domains of the respiratory syncytial virus (RSV) fusion (F) protein and the parainfluenza virus type 3 (PIV-3) hemagglutinin-neuraminidase (HN) protein in insect cells using the baculovirus expression system. The yield of the soluble chimeric FRSV-HNPIV-3 protein could be increased approximately 2-fold by using Trichoplasia ni (High Five) insect cells in place of Spodoptera frugiperda (Sf9) for expression. The chimeric protein, purified from the supernatant of baculovirus-infected High Five cells by immunoaffinity chromatography was correctly processed at the F2-F1 proteolytic cleavage site. Immunochemical analysis of the chimera with a panel of anti-F and anti-HN monoclonal antibodies suggested that the antigenicity of the major F and HN neutralization epitopes of the chimeric protein was preserved. Immunization of cotton rats with two 1 or 10 micrograms doses of the chimeric protein adsorbed to aluminum phosphate elicited strong PIV-3 specific HAI responses as well as PIV-3 and RSV specific neutralizing antibodies, and at either dose completely protected against challenge with live RSV and PIV-3.
Amino Acid Sequence↗
Structure of a pertussis toxin-sugar complex as a model for receptor binding.
Pertussis toxin is an exotoxin from the bacterium Bordetella pertussis which is important the pathogenesis of whooping cough and the generation of a protective immune response. The diverse biological activities of the toxin depend on its ability to recognize carbohydrate-containing receptors on a wide variety of eukaryotic cells. We present here the crystal structure of pertussis toxin complexed with a soluble oligosaccharide from transferrin. Binding sites for the terminal sialic acid-galactose moiety are revealed on both subunits S2 and S3 of the B-oligomer. Identification of amino acid residues involved in receptor binding will improve the design of genetically inactivated toxins for use in new acellular whooping cough vaccines.
Bacterial Vaccines↗
Mouse neurovirulence determinants of poliovirus type 1 strain LS-a map to the coding regions of capsid protein VP1 and proteinase 2Apro.
Poliovirus type 1 strain LS-a [PV1(LS-a)] is a OV variant adapted to mice by multiple passages through mouse and monkey tissues. To investigate the molecular basis underlying mouse neurovirulence of PV1(LS-a), a cDNA of the viral genome containing nucleotides 112 to 7441 was cloned, and the nucleotide sequence was determined. Compared with that of the mouse avirulent progenitor PV1(Mahoney), 54 nucleotide changes were found in the genome of the PV1(LS-a) virus, resulting in 20 amino acid substitutions in the virus polyprotein. Whereas the nucleotide changes were scattered throughout the genome, the amino acid substitutions were largely clustered in the capsid proteins and, to a certain extent, in the virus proteinase 2Apro. By in vitro mutagenesis, PV1(LS-a)-specific capsid mutations were introduced into a cDNA clone of PV1(Mahoney). We show that neither the individual amino acid mutations nor combinations of mutations in the region encoding VP1 conferred to PV1(Mahoney) the mouse-adapted phenotype of PV1(LS-a). Chimeric cDNA studies demonstrated that a recombinant type 1 virus containing the PV1(LS-a) sequence from nucleotide 2470 to nucleotide 3625 displayed a neurovirulent phenotype in mice. Further dissection of this region revealed that mouse neurovirulence of PV1(LS-a) was determined by multiple mutations in regions encoding both viral proteinase 2Apro and capsid protein VP1. The mouse neurovirulent viruses, PV1(LS-a), W1-M/LS-Pf [nucleotides 496 to 3625 from PV1(LS-a)], and W1-M/LS-NP [nucleotides 2470 to 3625 from PV1(LS-a)], showed increased sensitivity to heat treatment at 45 degrees C for 1 h. Surprisingly, the thermolabile phenotype was also displayed by a recombinant of PV1(Mahoney) carrying a PV1(LS-a) DNA fragment encoding the N-terminal portion of 2Apro. This suggests that base substitutions in the region encoding 2Apro affected capsid stability, thereby contributing to the neurovirulence of the virus in mice.
Animals↗