- Volume 139, Issue 3, 1993
Volume 139, Issue 3, 1993
- Biochemistry
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Purification and Properties of an Extracellular Aminopeptidase from Streptomyces Lividans 1326
More LessStreptomyces lividans was investigated for extracellular proteinases. The major extracellular proteinase activity detected under all conditions tested was l-leucine aminopeptidase activity. Slight extracellular l-proline aminopeptidase activity was also detected. No clear evidence for the presence of serine proteinases in S. lividans culture broths was found using several different methods. The major extracellular proteinase of S. lividans, i.e. the l-leucine aminopeptidase, was purified 33-fold to homogeneity. The purified enzyme was found by SDS-PAGE to have an M r of 34000. The purified enzyme had a final specific activity of 3·6 units mg−1, a K m for l-leucine-p-nitroanilide of 300 μm and a V max of 4·2 μmol min−1 mg−1. The pure enzyme did not exhibit proteolytic activity on azocasein or l-proline-p-nitroanilide, substrates for other proteinase activities observed in crude extracts of S. lividans.
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Identification, Genetic and Biochemical Analysis of Genes involved in Synthesis of Sugar Nucleotide Precursors of Xanthan Gum
More LessA genetic and biochemical analysis of Xanthomonas campestris chromosomal functions required for xanthan polysaccharide synthesis (xps) was undertaken. Seven xps DNA regions were isolated after conjugation of chemically induced non-mucoid mutants with a genomic library of X. campestris DNA. No overlapping segments between regions were detected, based on physical mapping, indicating the unlinked character of these regions. Clones complementing several different mutants belonging to the same region contained overlapping segments of X. campestris chromosomal DNA. Complementation and biochemical analysis, and DNA mapping were used to identify and characterize xpsIII, IV and VI DNA regions. Mutants in these three regions were able to synthesize both lipid intermediates and xanthan gum in vitro when sugar nucleotides were provided as substrates. HPLC analysis of the intracellular sugar nucleotide content showed that the XpsIII group comprises two different classes of mutants: XpsIIIA, defective in UDP-glucose, UDP-glucuronic acid and GDP-mannose, and XpsIIIB, defective in GDP-mannose. XpsIV mutants were defective in UDP-glucose and UDP-glucuronic acid, and XpsVI mutants were defective only in UDP-glucuronic acid. Analysis of enzyme activities involved in the synthesis of UDP-glucose, GDP-mannose and UDP-glucuronic acid indicated that the xpsIIIA region affects the activity of the phosphoglucomutase/phosphomannomutase enzyme, and the xpsIIIB region affects the mannoisomerase/ phosphomannoisomerase activities. The xpsIV mutations affect the activity of the UDPG-pyrophosphorylase enzyme, and the xpsVI mutations affect the activity of the UDPG-dehydrogenase enzyme.
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Positional distribution of fatty acids, and molecular species of polar lipids, in the diatom Phaeodactylum tricornutum
More LessEach of the four main polar lipids from Phaeodactylum tricornutum UTEX 640, monogalactyosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), sulphoquinovosyldiacylglycerol (SQDG) and phosphatidylcholine (PC), was separated into its molecular species by reverse-phase HPLC, and the positional distribution of fatty acids in each species was determined. Numbers of separated peaks in each lipid class were: MGDG, 10; DGDG, 7; SQDG, 10; and PC, 11. Eicosapentaenoic acid (EPA) was present in 20 of the 45 molecular species but predominated in the MGDG and DGDG classes, where 13 of the proposed structures contained EPA. EPA was always located in the sn-1 position except in two lipid species, MG5 and PC2, where it was present at both the sn-1 and sn-2 locations. The predominant polar lipid molecular species found in P. tricornutum UTEX 640 were (mg total fatty acids per g dry weight of biomass) 20:5–16:4–MG, 41·2; 20:5–16:1–DG, 21·0; 16:1–16:1–SQ, 18·2; and 20:5–16:1–MG, 18·0. [Structure indicates fatty acid at sn-1 position - fatty acid at sn-2 position-carbohydrate component at sn-3 position of the glycerol molecule. Abbreviations: 20:5, EPA; 16:4, hexadecatetraenoic acid; 16:1, palmitoleic acid; MG, monogalactose; DG, digalactose; SQ, sulphoquinovose.]
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Further Characterization of the Assimilatory Nitrate Reductase from the Yeast Candida Nitratophila
More LessNitrate reductase from the yeast Candida nitratophila was found to contain one molecule of cytochrome b 557 and one atom of molybdenum per subunit. FAD/haem-dependent diaphorase activity (haem domain) was associated with a 40 kDa tryptic fragment of the subunit. The 50 amino-terminal residues of this fragment were determined, and the sequence did not show significant similarity to deduced sequences of other nitrate reductases previously published. Increasing ionic strength in vitro had a stimulatory effect on enzymic activity via stimulation of the molybdenum-dependent terminal nitrate-reducing activity. Stimulation of activity by exogenous protein (bovine serum albumin or casein) also appeared to be an ionic effect. Stimulation of catalytic activity by phosphate was a separate effect.
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Purification and Partial Characterization of Acid Phosphatase from Candida Lipolytica
More LessNon-specific acid phosphatase from Candida lipolytica cells was purified 111-fold by chromatography on DEAE-cellulose and gel filtration on Sephadex G-100 and Sepharose 4B. The enzyme is a glycoprotein containing 67% neutral sugars. The molecular mass of the highly purified acid phosphatase was found to be approximately 95 kDa by both SDS-PAGE and gel filtration. The pH and temperature optima were 5·8 and 55 °C, respectively. The enzyme was stable at pH values between 3·5 and 5·5 and at temperatures up to 60 °C. The purified phosphatase had a K m value of 364 mm for p-nitrophenyl phosphate and showed broad substrate specificity.
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Investigation of a Killer Strain of Zygosaccharomyces Bailii
More LessThe yeast Zygosaccharomyces bailii strain 412 was found to liberate a killer toxin (KT412) lethal to sensitive strains of Saccharomyces cerevisiae and Candida glabrata. Culture supernatants of the killer strain were concentrated by ultrafiltration and the extracellular protein was purified by gel filtration and ion-exchange chromatography. Gel filtration and SDS-PAGE of the electrophoretically homogeneous killer protein indicated an apparent molecular mass of 10 kDa. The killer toxin KT412 is probably not glycosylated since it did not show any detectable carbohydrate structures. KT412 was bound to sensitive but not to resistant yeast cells. The mannan, and not the glucan, fraction of the cell wall of the sensitive yeast was the primary target for the killer toxin binding. The killer strain Z. bailii 412 contained three double-stranded RNA plasmids of 1·9, 2·9 and 4·0 kb. Curing by cycloheximide resulted in the concomitant loss of killer activity and the 1·9 kb dsRNA species that is therefore regarded as equivalent to the killer-toxin-coding M-plasmids of S. cerevisiae.
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Characterization and Complementation of Mutants of Methylophilus Methylotrophus that have Thermolabile Forms of Proteins Involved in C1 Metabolism
More LessTwo temperature-sensitive mutants of Methylophilus methylotrophus have been isolated and characterized. The first, NH-4, had a temperature-sensitive defect in methylamine oxidation and was unable to utilize methylamine as sole carbon and nitrogen source at 42 °C. The activities of the methylamine oxidation system and methylamine dehydrogenase in cells grown on methylamine at 30 °C were much more thermolabile than those of the wild-type. Furthermore, the affinity of the mutant enzyme for methylamine was lower than that of the wild-type enzyme. These results suggest that NH-4 produces a mutant enzyme with an altered conformation which is more susceptible to thermal denaturation than the wild-type enzyme. Surprisingly, this mutant could grow at 42 °C on media containing methylamine if an alternative carbon or nitrogen source was available. The methylamine oxidation system of whole cells grown under these conditions was not inactivated at 42 °C. The second mutant, NH-7, was unable to grow at the restrictive temperature on media containing either methanol or methylamine as sole carbon source. It contained thermolabile forms of methanol and methylamine dehydrogenases and cytochrom c L. This phenotype could be due to a mutation in a gene essential for the production of mature forms of these periplasmic proteins, which are involved in C1 metabolism. Cosmid pAD833, which has previously been shown to carry genes involved in methanol oxidation (mox genes), complemented both NH-4 and NH-7. Subcloning indicated that the gene which complemented NH-7 was within a 3 kbp region which contained at least two mox genes. This region was near an 8 kbp region containing the gene which complemented mutant NH-4.
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A Triacyltrehalose Containing 2-Methyl-Branched Unsaturated Fatty Acyl Groups Isolated from Mycobacterium Fortuitum
More LessA variety of glycolipids were found in a collection of strains of Mycobacterium fortuitum and two patterns were established by thin-layer chromatography. A compound present in all the strains studied was identified as 2,3,4-triacyltrehalose and its overall structure determined by infrared spectroscopy, nuclear magnetic resonance spectroscopy and gas-liquid chromatography-mass spectrometry. Fatty acyl groups present in this molecule were identified as tetradecanoyl, hexadecenoyl, hexadecanoyl, octadecenoyl, octadecanoyl and a variety of 2-methyl-branched unsaturated (α-methyl, α,β-unsaturated) acyl groups. The 2-methyl-branched compounds ranged from 17 to 21 carbon atoms, the most abundant being 2-methyloctadecen-2-oyl. Trehalose was the only sugar detected in the glycolipid. This substance immunoreacted with IgG and IgM present in sera from tuberculosis patients, as demonstrated by an enzyme-linked immunosorbent assay.
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- Biotechnology
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Changes in Lipid Composition and Arachidonic Acid Turnover during the Life Cycle of the Yeast Dipodascopsis Uninucleata
More LessUngerminated ascospores of Dipodascopsis uninucleata contained 18 times more lipid (5·5% dry wt) than germinated cells; the lipid comprised 58% (w/w) glycolipids, 28% (w/w) neutral lipids (mainly triacylglycerols) and 14% (w/w) phospholipids (mainly phosphatidylcholine and phosphatidylethanolamine). During germination the absolute amounts of all three lipid fractions fell sharply but, during the subsequent initiation of hyphal growth, the amount of phospholipids increased. As these hyphae began to differentiate for the sexual stage of the life cycle, the amount of neutral lipid then increased. The fatty acyl groups of the glyco-, neutral and phospholipid fractions throughout the life cycle were mainly palmitate (16:0), oleate (18:1) and linoleate (18:2). The percentage of 16:0 remained constant during the life cycle while the relative amounts of 18:2 plus α-linolenate (18:3) in the glyco-,neutral and phospholipid fractions first increased during initiation of growth and then decreased during the onset of differentiation. The opposite trend occurred with 18:1. When [3H]arachidonic acid (ARA) and [1-14C]18:1 were fed separately to D. uninucleata, both were rapidly incorporated into phospholipids. Highest incorporation of ARA was in the growth phase; during the onset and remainder of the differentiation phase, the amount of ARA decreased in this fraction. Incorporation of 18:1 increased during growth and differentiation, with a significant proportion (49% to 57%) being incorporated into triacylglycerols compared to a much smaller proportion (12% to 17%) of ARA.
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- Genetics And Molecular Biology
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Primary Structure, Partial Purification and Regulation of Key Enzymes of the Acetyl Cycle of Arginine Biosynthesis in Bacillus Stearothermophilus: Dual Function of Ornithine Acetyltransferase.
A 3·4 kb EcoRI fragment, cloned in E. coli, that carries part of a cluster of genes encoding arginine biosynthetic functions of the thermophilic bacterium Bacillus stearothermophilus, was sequenced on both strands. The sequence consists of a truncated argC gene, an argJ region encoding a polypeptide with both N-acetylglutamate synthase and ornithine acetyltransferase activities, the argB gene and the N-terminal part of argD. The argB gene encodes a 258-amino-acid polypeptide with a deduced M r of 26918. A very high and thermostable N-acetylglutamate 5-phosphotransferase activity was detected in extracts of E. coli argB mutants transformed with the 3·4 kb fragment on a plasmid. A polypeptide band of M r 27000 was detected by SDS-PAGE of heat-treated extract from such a strain. Both N-acetylglutamate synthase and ornithine acetyltransferase are encoded by the same 1290 bp open reading frame. The deduced sequence of 410 amino acids corresponds to a peptide of M r 43349. The subcloned B. stearothermophilus argJ can complement a double argA argE E. coli mutant to prototrophy. Gel-filtration of a heat-treated extract of the complemented double mutant E. coli host showed that N-acetylglutamate synthase and ornithine acetyltransferase activities co-elute in a single peak corresponding to M r 110000. Both activities were also heat-inactivated at the same temperature and strongly inhibited by ornithine. These results suggest that both activities can be ascribed to a single protein.
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Molecular and Enzymological Evidence for Two Classes of Fumarase inBacillus Stearothermophilus(var.Non-Diastaticus)
More LessThe gene (fumA Bst) encoding an oxygen-labile fumarase of Bacillus stearothermophilus has been cloned and sequenced. The structural gene (1542 bp) encodes a product (FumABst) of M r 56788 containing 514 amino acid residues. The amino acid sequence is 23% identical (37% similar) to FumA and FumB, the labile [4Fe-4S]-containing fumarases (Class I enzymes) of Escherichia coli. It exhibits no significant similarity to FumC and CitG, the stable fumarases (Class II enzymes) of E. coli and Bacillus subtilis (respectively). Enzymological studies indicated that FumABst resembles the iron-sulphur-containing fumarases in being dimeric (M r 2 × 58500), oxygen labile and partially reactivated by Fe2+plus DTT. The fumA Bst gene is the first gene encoding a Class I fumarase to be characterized in any organism other than E. coli. Enzymological and DNA-hybridization studies further indicated that B. stearothermophilus resembles E. coli in containing an oxygen-stable fumarase (Class II enzyme). Sequence comparisons revealed significant similarities between the Class I fumarases and the products of adjacent open-reading frames (orfZ1 and orfZ2) located upstream of the macromolecular synthesis operon (rpsU-dnaG-rpoD) at 67 min in the E.coli linkage map. Located downstream of fumA Bst, there is an unidentified gene (orf2), which is homologous to the rhizobial nodB genes involved in the initiation of root nodule formation.
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Putrescine Oxidase of Micrococcus Rubens: Primary Structure and Escherichia Coli
More LessThe flavin adenine dinucleotide (FAD)-containing putrescine oxidase of Micrococcus rubens catalyses the oxidative deamination of putrescine. The amino acid sequences of the NH2-termini of the mature enzyme and lysyl-endopeptidase-generated fragments were determined for preparation of synthetic oligonucleotides as hybridization probes for cloning. A 4·4 kb BamHI fragment which contained DNA sequences hybridizing to the probes was cloned in pUC19 in Escherichia coli. The nucleotide sequence together with the determined amino acid sequences revealed that this enzyme consists of 480 amino acids (M r 52000) and contains an FAD-binding consensus sequence at its NH2-terminal portion. In front of the transcriptional start point, which is 28 bases upstream of the initiation codon as determined by primer extension, −35 and −10 sequences similar to typical prokaryotic promoter consensus sequences are present. E. coli JM109 containing the putrescine oxidase gene just downstream of the lac promoter in pUC18 produced a large amount of this protein when grown at 37 °C but in the enzymically inactive form of inclusion bodies. However, cultivation of the recombinant E. coli cells at temperatures below 30°C led to production of active enzyme (20 times as much as produced by the original M. rubens strain).
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Properties of Genes Involved in the Control of Isocitrate Lyase Production in Aspergillus nidulans
More LessThe interaction between genes of Aspergillus nidulans conferring constitutive synthesis of isocitrate lyase (iclcA and iclcB) and fluoroacetate resistance (facB) has been investigated. Although facB mutants are unable to induce the glyoxylate cycle enzyme isocitrate lyase in response to acetate as sole carbon source, this phenotype was suppressed in recombinants of the type iclc;facB. The iclcA and iclcB mutations do not alter significantly the activities of eight enzymes of intermediary metabolism assayed. We conclude that the iclc genes are probably bona fide isocitrate lyase regulatory genes.
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Investigation of Thermolabile Variants of the Methanol and Methylamine Dehydrogenases of Methylophilus Methylotrophus and the Effect of an 11·5 kbp Region of the Chromosome on the Stability of these enzymes
More LessThe thermal stabilities in vitro of the methylamine and methanol dehydrogenases of Methylophilus methylotrophus varied, depending on the conditions in which the organism was grown. Methylamine dehydrogenase activity was more stable in extracts of cells grown on methylamine plus NH+ 4 or on methanol plus methylamine than when methylamine provided the sole carbon and nitrogen source. In contrast, the methanol dehydrogenase activity in extracts of methylamine-grown cells was more stable than that from cells grown on medium containing methanol with either NH+ 4 or methylamine as the nitrogen source. The stability of thermolabile forms of the dehydrogenases present in extracts of mutants which have temperature-sensitive defects in the oxidation of C1 compounds also varied with the growth conditions. When cosmid pAD833, which complemented these temperature-sensitive mutants, was present during growth of the wild-type strain on methylamine, the thermal stabilities of both methylamine and methanol dehydrogenases increased. However, the effects of subclones of pAD833 were complex and our results indicate that the DNA region carried on this cosmid encodes gene products which can both increase and decrease the in vitro thermal stability of enzymes involved in C1 metabolism.
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A Comparison of the Multiple Alleles of xylS Carried by TOL Plasmids pWW53 and pDK1 and its Implications for their Evolutionary Relationship
Both of the independently isolated TOL plasmids pWW53 and pDK1 contain multiple regions homologous to the xylS regulatory gene of the archetypal TOL plasmid pWW0. The three homologues on pWW53 vary in the extent of their homology to xylS pWW0. xylS1 pWW53 is 99% identical to xylS pWW0 and is located relative to the single copy of xylR pWW53 in exactly the same way as xylS and xylR on pWW0. The DNA sequence of xylS3 pWW53 is 87% identical to the xylS pWW0 sequence within the coding region but the non-coding DNA upstream is not homologous. There is a frame-shift change at the end of the coding region which causes the C terminus of XylS3pWW53 to be extended by an additional 10 amino acids relative to XylSpWW0. xylS2 pWW53 is anomalous and appears to encode a truncated pseudogene lacking the first 525 bases found in the other xylS genes. Evidence is presented to show that both xylS1 pWW53 and xylS3 pWW53 act as regulators of meta pathway operons. Plasmid pDK1 carries two homologues of xylS. xylS1 pDK1 is functional and is a hybrid gene: its 5� end and the upstream sequences are highly homologous to both xylS pWW53 and xylS pWW0, whereas its 3� end is identical to xylS3 pWW53. The sequence of xylS2 pDK1 is identical to that of the anomalous truncated xylS2 pWW53. Comparison of the organization and the restriction maps of the xyl catabolic operons on pDK1 and pWW53, together with the nucleotide sequences presented here, indicates that the catabolic DNA on pDK1 has derived from a replicon on which the xyl genes are organized similarly to pWW53 and that a genetic rearrangement has taken place involving a reciprocal recombination internal to two of its xylS homologues.
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A Mobilizable Shuttle Vector for the Cyanobacterium Plectonema Boryanum
More LessPlasmid pSUP5011 contains a pMB1 origin of replication, an origin of transfer (oriT), and genes encoding resistance to the antibiotics ampicillin, chloramphenicol and kanamycin. pSUP5011 was conjugally mobilized from Escherichia coli into the non-heterocystous, filamentous, nitrogen-fixing cyanobacterium Plectonema boryanum UTEX 594 in the presence of a helper plasmid, RP4. Transconjugant cyanobacteria selected for resistance to kanamycin, ampicillin and chloramphenicol showed a variety of DNA rearrangements in pSUP5011. One such plasmid continued to show characteristic rearrangements following subsequent transfers into the cyanobacterium. A stable plasmid useful as a shuttle vector was isolated.
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Cloning and Sequencing of the Gene which Encodes the Highly Inducible Acetamidase of Mycobacterium Smegmatis
More LessThe acetamidase of Mycobacterium smegmatis NCTC 8159 was purified, and the sequences of its amino-terminus and of two peptides obtained by proteolysis of the protein were obtained. A DNA fragment including the amidase structural gene was cloned in Escherichia coli, using oligonucleotide probes designed on the basis of the peptide sequences and a codon usage table calculated from published sequences of nine protein-antigen-encoding genes of the Mycobacterium tuberculosis complex. Sequence analysis of the cloned DNA revealed that the amidase gene encoded 406 amino acid residues. The nucleotide sequence close to and upstream of the amidase gene contained a probable ribosome-binding site but no identifiable promoter sequences. Three additional potential open-reading frames were found upstream of and very close to the amidase gene, with consensus ‘−35’ and ‘−10’ promoter sites between the first and second of these. It is hoped that the highly inducible expression of the acetamidase gene can be exploited to allow regulated expression of other genes cloned in mycobacteria.
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Characterization of Two Different Types of Resistance Genes Among Producers of Fortimicin-Group Antibiotics
More LessFortimicin-A (FTM-A; astromicin)-resistance genes (fmr genes) isolated from six producers of the FTM-group of antibiotics were analysed. These genes could be classified into two types by the resistance profiles to aminoglycoside antibiotics and by their DNA homologies. Three genes, fmrT from the istamycin producer Streptomyces tenjimariensis ATCC 31603, fmrS from the sannamycin producer Streptomyces sannanensis IFO 14239 and fmrH from the sporaricin producer Saccharopolyspora hirsuta ATCC 20501, conferred resistance to FTM-A, kanamycin (Km) and neomycin B (Nm-B), but not to gentamicin (Gm). The other three genes, fmrO from the FTM-A producer Micromonospora olivasterospora ATCC 21819, fmrM from the antibiotic SF-2052 producer Micromonospora sp. SF-2098 (ATCC 31580) and fmrD from the dactimicin producer Dactylosporangium matsuzakiense ATCC 31570, conferred resistance to FTM-A, Km and Gm, but not to Nm-B. No DNA homology was detected between the two types of the resistance genes in Southern-blot analysis. The present results revealed that, in spite of the similarity of their biosynthesis genes, there are at least two different types of resistance genes among the FTM-group antibiotic producers.
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A Macrolide–Lincosamide–Streptogramin B Resistance Determinant from Bacillus anthracis 590: Cloning and Expression of ermJ
More LessThe inducible macrolide-lincosamide-streptogramin B resistance determinant, ermJ, from Bacillus anthracis 590 was cloned in Escherichia coli CSH26. The DNA sequence of ermJ was similar to that of ermK or ermD from B. licheniformis, suggesting that ermK-like genes have been distributed in Bacillus strains by transposition. Expression of ermJ was achieved in a B. subtilis minicell system, and the rRNA methyltransferase product of ermJ was purified. The molecular mass of the enzyme was 58 kDa, and it was concluded to be a homodimer. Its biochemical characteristics were different from those of ermC methyltransferase.
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- Pathogenicity And Medical Microbiology
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Cell-Surface Location of Listeria-Specific Protein p60-Detection of Listeria Cells by Indirect Immunofluorescence
More LessA specific polyclonal antiserum was prepared against a gel-purified 60 kDa extracellular protein of Listeria monocytogenes ATCC 19111 corresponding to protein p60 previously detected in culture broths of L. monocytogenes strains Mackaness and EGD [Kuhn, M. & Goebel, W. (1989), Infection and Immunity 57, 55–61]. Indirect immunogold labelling combined with transmission electron microscopy and high-resolution scanning electron microscopy were used toinvestigate the location and distribution of p60 on the bacterial cell surface. In bacteria grown to the early stationary phase about 25% of the extracellular protein was estimated to be associated with the cell surface. The anti-p60 antiserum proved to be Listeria-specific. In an indirect immunofluorescence test the antiserum reacted with Listeria strains representing all species and different serotypes, except L. seeligeri, L. welshimeri, L. grayi and L. murrayi. No immunological cross-reactions were observed with 27 strains of bacteria from 16 other genera. The value of the anti-p60 antiserum in developing a diagnostic assay for Listeria cells in environmental samples and foods is discussed.
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