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Biomedical subjects

R Munson

Publications and source records attributed to R Munson.

At least 19 recordsLinked to original sources
PubMed1992

Outer membrane proteins P1 and P2 of Haemophilus influenzae type b: structure and identification of surface-exposed epitopes.

The outer membrane proteins (OMPs) P1 and P2 of Haemophilus influenzae type b exhibit molecular size and antigenic variation. Their structural genes have been cloned from prototype isolates of the most common disease-producing clonal groups. The derived amino acid sequences of P1 from strains of OMP subtypes 1H, 3L, and 6U have three variable regions between highly conserved regions. An immunodominant surface-exposed epitope was identified near the carboxyl terminus of P1 proteins from subtype 1H and 3L strains. The P2 genes from subtype 1H, 1L, and 3L isolates were identical. The P2 gene sequence from a subtype 6U isolate differs from the subtype 1H P2 gene by 13 nucleotides, resulting in 10 amino acid changes. The P2 gene from a subtype 2L isolate differs by 1 nucleotide from the subtype 1H P2 gene, resulting in 1 amino acid change at position 166. Two surface-exposed epitopes of OMP P2 were identified, one each between residues 158 and 174 and residues 319 and 341.

Animals↗
PubMed1991

Comparison of the structure of the genes for outer membrane proteins P1 and P2 of Haemophilus influenzae type b.

Size and antigenic heterogeneity have been recognized in both outer membrane protein P1 and outer membrane protein P2 of Haemophilus influenzae type b. To determine the molecular basis for these differences, we have cloned and sequenced the structural genes for OMPs P1 and P2 from prototype isolates with the OMP subtypes 1H, 3L and 6U. The nucleotide and derived amino acid sequences of the P1 genes are characterized by three variable regions dispersed between highly conserved regions. The nucleic acid and derived amino acid sequences of the P2 genes are also highly conserved. The P2 genes from OMP subtype 1H and 3L isolates are identical. The sequence of the 6U gene differs by 13 nucleotides, resulting in 10 amino acid changes.

Bacterial Outer Membrane Proteins↗
PubMed1991

Mapping of B-cell epitopes on the outer membrane P2 porin protein of Haemophilus influenzae by using recombinant proteins and synthetic peptides.

The P2 protein of Haemophilus influenzae type b has a porin activity and is the most abundant protein in the outer membrane. We have employed fusion protein constructs and synthetic peptides along with monoclonal antibodies to map B-cell epitopes in this protein. A linear, surface-exposed epitope was identified between residues 158 and 174. A second surface-exposed epitope was identified near the carboxy-terminal end of the protein (residues 319 to 341). Two additional B-cell epitopes were identified. One was localized between residues 28 and 55, whereas the other was located between residues 148 and 174. These epitopes were not present on the surface of intact H. influenzae cells. Thus, four distinct immunogenic and antigenic regions on the P2 protein have been identified.

Amino Acid Sequence↗
PubMed1991

Molecular cloning, expression, and sequence of the pilin gene from nontypeable Haemophilus influenzae M37.

Nontypeable Haemophilus influenzae M37 adheres to human buccal epithelial cells and exhibits mannose-resistant hemagglutination of human erythrocytes. An isogenic variant of this strain which was deficient in hemagglutination was isolated. A protein with an apparent molecular weight of 22,000 was present in the sodium dodecyl sulfate-polyacrylamide gel profile of sarcosyl-insoluble proteins from the hemagglutination-proficient strain but was absent from the profile of the isogenic hemagglutination-deficient variant. A monoclonal antibody which reacts with the hemagglutination-proficient isolate but not with the hemagglutination-deficient isolate has been characterized. This monoclonal antibody was employed in an affinity column for purification of the protein as well as to screen a genomic library for recombinant clones expressing the gene. Several clones which contained overlapping genomic fragments were identified by reaction with the monoclonal antibody. The gene for the 22-kDa protein was subcloned and sequenced. The gene for the type b pilin from H. influenzae type b strain MinnA was also cloned and sequenced. The DNA sequence of the strain MinnA gene was identical to that reported previously for two other type b strains. The DNA sequence of the strain M37 gene is 77% identical to that of the type b pilin gene, and the derived amino acid sequence is 68% identical to that of the type b pilin.

Amino Acid Sequence↗
PubMed1989

Vector analysis of three-dimensional evoked potentials: eccentric dipoles.

The quantitative description of three-dimensional cerebral evoked potentials is extended to include eccentric dipolar sources. Eccentricity-related distortions in dipole orientation and magnitude are assessed. The use of nonstandard montages, the prediction of topographic surface maps, dynamic analysis, and theoretical mechanisms of planar segment formation are discussed.

Brain↗
PubMed1989

Diversity of the outer membrane protein P2 gene from major clones of Haemophilus influenzae type b.

In previous studies, it has been demonstrated that outer membrane protein P2 from Haemophilus influenzae type b has porin activity and that antibody directed against P2 is protective in an infant rat bacteraemic model. Outer membrane protein subtyping has been employed to subclassify type b Haemophilus isolates. Strain MinnA has the outer membrane protein subtype 1H and is representative of the dominant clonal group of disease-producing isolates in the United States. In the present study, the P2 gene from strain MinnA was employed to probe EcoRI- and Pvull-digested chromosomal DNA from 24 Haemophilus influenzae type b isolates representative of the common outer membrane protein subtype groups observed throughout the world. Restriction fragment length polymorphisms were identified for the members of the outer membrane protein subtype 3L group, but not for the other subtypes examined. The P2 gene from each of four prototype isolates was then cloned, sequenced and compared to the previously reported sequence of the strain MinnA gene. The P2 gene from each of two isolates with the outer membrane protein subtype 3L was identical to the MinnA P2 sequence. The P2 gene from a subtype 2L isolate differed by a single nucleotide and the gene from a subtype 6U isolate differed by 13 nucleotides. Thus, the P2 protein is highly conserved among type b isolates.

Amino Acid Sequence↗
PubMed1989

Molecular cloning, expression, and primary sequence of outer membrane protein P2 of Haemophilus influenzae type b.

The structural gene for the porin of Haemophilus influenzae type b, designated outer membrane protein P2, was cloned, and the DNA sequence was determined. An oligonucleotide probe generated by reverse translation of N-terminal amino acid sequence data from the purified protein was used to screen genomic DNA. The probe detected a single EcoRI fragment of approximately 1,700 base pairs which was cloned to lambda gt11 and then into M13 and partially sequenced. The derived amino acid sequence indicated that we had cloned the N-terminal portion of the P2 gene. An overlapping approximately 1,600-base-pair PvuII genomic fragment was cloned into M13, and the sequence of the remainder of the P2 gene was determined. The gene for P2 was then reconstructed under the control of the T7 promoter and expressed in Escherichia coli. The N-terminal sequence of the purified protein corresponds to residues 21 through 34 of the derived amino acid sequence. Thus, the protein is synthesized with a 20-amino-acid leader peptide. The Mr of the processed protein is 37,782, in good agreement with the estimate of 37,000 from sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

Amino Acid Sequence↗
PubMed1989

Comparative analysis of the structures of the outer membrane protein P1 genes from major clones of Haemophilus influenzae type b.

P1 outer membrane proteins from Haemophilus influenzae type b are heterogeneous antigenically and with respect to apparent molecular weight in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. For determination of the molecular basis for the differences in the P1 proteins, the genes for the P1 proteins from strain 1613, representative of outer membrane protein subtype 3L, and strain 8358, representative of outer membrane protein subtype 6U, were cloned, sequenced, and compared with the previously reported gene for the P1 protein from strain MinnA, a strain with the outer membrane protein subtype 1H. These prototype strains are representatives of the three major clonal families of H. influenzae type b responsible for invasive disease in diverse areas of the world. The nucleotide sequences of the P1 genes from strains 1613 and 8358 were 94 and 90% identical to the MinnA sequence, respectively. The derived amino acid sequences were 91 and 86% identical, respectively. Heterogeneity between the MinnA and 1613 proteins was largely localized to two short variable regions; the protein from strain 8538 contained a third variable region not observed in the other P1 proteins. Thus, the outer membrane protein P1 genes are highly conserved; the variable regions may code for the previously demonstrated strain-specific antigenic determinants.

Amino Acid Sequence↗
PubMed1989

Isolation and characterization of a mutant of Haemophilus influenzae type b deficient in outer membrane protein P1.

The gene for outer membrane protein P1 of Haemophilus influenzae type b has been previously cloned and expressed in Escherichia coli. To investigate the physiologic role of the P1 protein, the cloned P1 gene was insertionally inactivated with the Tn5 derivative Tn5tac1, and an isogenic P1-deficient Haemophilus mutant was then generated by transformation with linearized plasmid DNA containing the insertionally inactivated gene. The P1-deficient strain grew normally in vitro and induced bacteremia in the infant rat model.

Bacterial Outer Membrane Proteins↗
PubMed1988

Purification, cloning, and sequence of outer membrane protein P1 of Haemophilus influenzae type b.

Outer membrane protein P1 from Haemophilus influenzae type b MinnA was purified and partially characterized. Antiserum was generated against the purified protein and was used to immunologically screen a lamba EMBL3 genomic library prepared from strain MinnA DNA. A 4.2-kilobase-pair EcoRI-BamHI fragment containing the P1 gene was subcloned into pBR322. The recombinant protein was synthesized by Escherichia coli K-12, in which it localized to the outer membrane. The N-terminal sequence of the purified protein was determined and found to correspond to residues 23 through 36. The 22-amino-acid leader peptide had a typical structure, with two lysine residues near the amino terminus, a stretch of hydrophobic residues, and alanine residues at positions 20 and 22. The Mr of the processed protein was 47,752, which is in good agreement with the estimate of 50,000 from sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Putative -35 and -10 promoter sequences were identified upstream from the translational start site. Codon usage was examined and determined to be substantially different than the codon preference in E. coli.

Amino Acid Sequence↗
PubMed1984

The relation of P3b to prior events and future behavior.

A prediction paradigm was used to explore the relationship of the amplitude of the scalp-recorded event-related potential to the sequence of preceding signals and to preceding and subsequent behavior. P3b was found to be the only component which related systematically to prior sequence of signals. The CNV, P300E and Slow Wave were not affected by signal sequence. The P3b findings were the same for the emitted and evoked P3b, thus ruling out a sensory interpretation of the effect of signal sequence on P3b amplitude. Furthermore, it was found that signal sequence interacts with the subject's predictions in determining P3b amplitude. For signal discontinuations, P3b was large in amplitude regardless of what had been predicted. However, for signal continuations, P3b was small when continuations had been predicted, but large when discontinuations had been predicted. Finally, we found that for both correctly and incorrectly predicted signal continuations, larger P3bs were more likely than smaller P3bs to be followed by a prediction that the signal for the next trial would be different.

Adolescent↗
PubMed1984

Cardiopulmonary resuscitation at a community hospital with a family practice residency.

The cardiopulmonary resuscitation (CPR) experience of a family practice residency program within a community hospital was reviewed for the period of July 1, 1979, to June 30, 1981. CPR was attempted 300 times on 242 patients experiencing cardiopulmonary arrest. The emergency department and operating room were excluded from the study. Successful resuscitation was accomplished in 145 instances (48.3 percent). Short-term survival (survival for greater than 24 hours) occurred in 111 instances (37 percent). Thirty-four (14 percent) of the 242 patients resuscitated survived to be discharged from the hospital. The most common primary diagnosis of the patients experiencing cardiac arrest was coronary heart disease. The length of time of each of the code conditions was determined, and its relationship to overall survival rates was found to be inversely proportional. Advanced age did not adversely affect the final outcome of successful attempts. This study reaffirmed the expectation that consistently good results can be obtained if the physician, staff, and resuscitation team members are properly prepared and clear role delineation exists.

Adult↗
PubMed1982

Multiple controls for the synthesis of muscle-specific proteins in BC3H1 cells.

The regulation of the synthesis of muscle-specific proteins has been examined in BC3H1 cells, a smooth muscle-like cell line isolated by Schubert et al. (J. Cell Biol., 1974, 61: 398-413.). The synthesis of both creatine kinase and the acetylcholine receptor appear to be under dual control, a positive control due to cell-cell contact which increases the rate of synthesis of this protein, and a negative signal, elicited by serum components, that decreases the rate of synthesis of these proteins. Induction of muscle-specific proteins in BC3H1 cells is a reversible process and can be arrested after partial induction has taken place by the addition of serum or high-molecular-weight protein fraction from serum to these cells. The high-molecular-weight protein fraction from serum is not by itself mitogenic for Bc3H1 cells and cannot be replaced by a variety of known hormones (mitogenic factors).

Animals↗
PubMed1981

Why medicine cannot be a science.

My thesis is that, although medicine is scientific, it is not and can not become a science. After rejecting as flawed an argument attempting to show that medicine is already is science. I argue that a comparison of such basic, defining features as internal aims, criteria of success, and principles regulating the enterprises demonstrate that medicine and science are inherently different. I then argue that while it may be possible to reduce the cognitive content of medicine to biology, medicine itself cannot be reduced, for as an enterprise it possesses features that make it an inappropriate subject of reduction. I conclude by indicating four results that emerge from recognizing that medicine and science are basically distinct.

Medicine↗