Solubilization of potassium-bearing minerals by a wild-type strain of Bacillus edaphicus and its mutants and increased potassium uptake by wheat

2006 ◽  
Vol 52 (1) ◽  
pp. 66-72 ◽  
Author(s):  
Xia Fang Sheng ◽  
Lin Yan He
Keyword(s):  
Organic Acids ◽  
Type Strain ◽  
Wild Type Strain ◽  
Capsular Polysaccharide ◽  
Active Agent ◽  
Triticum Aestivum L ◽  
Wild Type ◽  
Bacterial Strains ◽  
Potassium Nutrition ◽  
Tartaric Acids

Two potassium (K)-bearing minerals, Nanjing feldspar and Suzhou illite, were used to investigate K mobilization by the wild-type strain NBT of Bacillus edaphicus, also labeled MPs+, selected for high activity in mobilizing potassium from minerals, and by four of its UV + LiCl mutants, MPs++, MPs+1, MPs+2, and MPs–. In liquid cultures, the five bacterial strains showed better growth on Suzhou illite than on Nanjing feldspar. Suzhou illite was the better potassium source for the growth of the wild type and the MPs++, MPs+1, and MPs+2 mutants. Solubilization of K from its sources by the wild-type NBT and the MPs++ mutant resulted mostly from the action of organic acids and capsular polysaccharides. Oxalic acid seemed to be a more active agent for the solubilization of Nanjing feldspar. Oxalic and tartaric acids were likely involved in the solubilization of Suzhou illite. The MPs– mutant did not produce any organic acid or capsular polysaccharide when grown on the above two K sources. In a pot experiment, wheat (Triticum aestivum L.) 'Yangmai-158' was grown in a yellow–brown soil that had low available K. After inoculation with bacterial strains, B. edaphicus NBT and its four mutants, MPs++, MPs+1, MPs+2, and MPs– (in separate tests), the root growth and shoot growth of wheat were significantly increased by B. edaphicus NBT and the mutants MPs++ and MPs+1. Bacterial inoculation also resulted in significantly higher N, P, and K contents of plant components. The bacteria were able to survive in the wheat rhizosphere soils after root inoculation.Key words: Bacillus edaphicus, potassium release, organic acids, potassium nutrition.

scholarly journals Role of Lung Epithelial Cells in Defense against Klebsiella pneumoniae Pneumonia

2002 ◽  
Vol 70 (3) ◽  
pp. 1075-1080 ◽  
Author(s):  
Guadalupe Cortés ◽  
Dolores Álvarez ◽  
Carles Saus ◽  
Sebastián Albertí
Keyword(s):  
Epithelial Cells ◽  
Klebsiella Pneumoniae ◽  
Type Strain ◽  
Pathogenic Bacteria ◽  
Wild Type Strain ◽  
Capsular Polysaccharide ◽  
Defense Mechanism ◽  
Lung Epithelial Cells ◽  
Wild Type ◽  
Lung Epithelial

ABSTRACT The airway epithelium represents a primary site for the entry of pathogenic bacteria into the lungs. It has been suggested for many respiratory pathogens, including Klebsiella pneumoniae, that adhesion and invasion of the lung epithelial cells is an early stage of the pneumonia process. We observed that poorly encapsulated K. pneumoniae clinical isolates and an isogenic unencapsulated mutant invaded lung epithelial cells more efficiently than highly encapsulated strains independent of the K type. By contrast, the unencapsulated mutant was completely avirulent in a mouse model of pneumonia, unlike the wild-type strain, which produced pneumonia and systemic infection. Furthermore, the unencapsulated mutant bound more epithelially produced complement component C3 than the wild-type strain. Our results show that lung epithelial cells play a key role as a host defense mechanism against K. pneumoniae pneumonia, using two different strategies: (i) ingestion and control of the microorganisms and (ii) opsonization of the microorganisms. Capsular polysaccharide avoids both mechanisms and enhances the virulence of K. pneumoniae.

scholarly journals Mutation of waaC, Encoding Heptosyltransferase I in Campylobacter jejuni 81-176, Affects the Structure of both Lipooligosaccharide and Capsular Carbohydrate

2006 ◽  
Vol 188 (9) ◽  
pp. 3273-3279 ◽  
Author(s):  
Margaret I. Kanipes ◽  
Erzsebet Papp-Szabo ◽  
Patricia Guerry ◽  
Mario A. Monteiro
Keyword(s):  
Campylobacter Jejuni ◽  
Type Strain ◽  
Insertional Mutagenesis ◽  
Lipid A ◽  
Wild Type Strain ◽  
Capsular Polysaccharide ◽  
Resonance Spectroscopy ◽  
Gas Liquid Chromatography ◽  
Wild Type ◽  
Isolation And Characterization

ABSTRACT Campylobacter jejuni 81-176 lipooligosaccharide (LOS) is composed of two covalently linked domains: lipid A, a hydrophobic anchor, and a nonrepeating core oligosaccharide, consisting of an inner and outer core region. We report the isolation and characterization of the deepest rough C. jejuni 81-176 mutant by insertional mutagenesis into the waaC gene, encoding heptosyltransferase I that catalyzes the transfer of the first l-glycero-d-manno-heptose residue to 3-deoxy-d-manno-octulosonic residue (Kdo)-lipid A. Tricine gel electrophoresis, followed by silver staining, showed that site-specific mutation in the waaC gene resulted in the expression of a severely truncated LOS compared to wild-type strain 81-176. Gas-liquid chromatography-mass spectrometry and nuclear magnetic resonance spectroscopy showed that the waaC LOS species lacked all sugars distal to Kdo-lipid A. Parallel structural studies of the capsular polysaccharides of the wild-type strain 81-176 and waaC mutant revealed loss of the 3-O-methyl group in the waaC mutant. Complementation of the C. jejuni mutant by insertion of the wild-type C. jejuni waaC gene into a chromosomal locus resulted in LOS and capsular structures identical to those expressed in the parent strain. We also report here the presence of O-methyl phosphoramidate in wild-type strain 81-176 capsular polysaccharide.

scholarly journals Comparison of the Host Responses to Wild-Type and cpsB Mutant Klebsiella pneumoniae Infections

2006 ◽  
Vol 74 (9) ◽  
pp. 5402-5407 ◽  
Author(s):  
Matthew S. Lawlor ◽  
Scott A. Handley ◽  
Virginia L. Miller
Keyword(s):  
Klebsiella Pneumoniae ◽  
Mouse Model ◽  
Type Strain ◽  
Wild Type Strain ◽  
Capsular Polysaccharide ◽  
Cytokine Production ◽  
Host Responses ◽  
Cellular Infiltration ◽  
Wild Type ◽  
Highly Virulent

ABSTRACT Previously, we established an intranasal mouse model of Klebsiella pneumoniae infection and validated its utility using a highly virulent wild-type strain and an avirulent capsular polysaccharide mutant. In the present study we compare the host responses to both infections by examining cytokine production, cellular infiltration, pulmonary histology, and intranasal immunization.

scholarly journals Fitness Cost of Rifampin Resistance in Neisseria meningitidis:In VitroStudy of Mechanisms Associated withrpoBH553Y Mutation

2015 ◽  
Vol 59 (12) ◽  
pp. 7637-7649 ◽  
Author(s):  
Roberta Colicchio ◽  
Chiara Pagliuca ◽  
Gabiria Pastore ◽  
Annunziata Gaetana Cicatiello ◽  
Caterina Pagliarulo ◽  
...  
Keyword(s):  
Type Strain ◽  
Wild Type Strain ◽  
Capsular Polysaccharide ◽  
Culture Media ◽  
Point Mutations ◽  
Clinical Isolates ◽  
Sequencing Analysis ◽  
Wild Type ◽  
Rifampin Resistance

ABSTRACTRifampin chemoprophylaxis againstNeisseria meningitidisinfections led to the onset of rifampin resistance in clinical isolates harboring point mutations in therpoBgene, coding for the RNA polymerase β chain. These resistant strains are rare in medical practice, suggesting their decreased fitness in the human host. In this study, we isolated rifampin-resistantrpoBmutants from hypervirulent serogroup C strain 93/4286 and analyzed their different properties, including the ability to grow/survive in different culture media and in differentiated THP-1 human monocytes and to compete with the wild-type strainin vitro. Our results demonstrate that differentrpoBmutations (H553Y, H553R, and S549F) may have different effects, ranging from low- to high-cost effects, on bacterial fitnessin vitro. Moreover, we found that the S549F mutation confers temperature sensitivity, possibly explaining why it is observed very rarely in clinical isolates. Comparative high-throughput RNA sequencing analysis of bacteria grown in chemically defined medium demonstrated that the low-cost H553Y substitution resulted in global transcriptional changes that functionally mimic the stringent response. Interestingly, many virulence-associated genes, including those coding for meningococcal type IV pili, porin A, adhesins/invasins, IgA protease, two-partner secretion system HrpA/HrpB, enzymes involved in resistance to oxidative injury, lipooligosaccharide sialylation, and capsular polysaccharide biosynthesis, were downregulated in the H553Y mutant compared to their level of expression in the wild-type strain. These data might account for the reduced capacity of this mutant to grow/survive in differentiated THP-1 cells and explain the rarity of H553Y mutants among clinical isolates.

scholarly journals Characterization of the Importance of Polysaccharide Intercellular Adhesin/Hemagglutinin of Staphylococcus epidermidis in the Pathogenesis of Biomaterial-Based Infection in a Mouse Foreign Body Infection Model

1999 ◽  
Vol 67 (5) ◽  
pp. 2627-2632 ◽  
Author(s):  
Mark E. Rupp ◽  
Joseph S. Ulphani ◽  
Paul D. Fey ◽  
Katrin Bartscht ◽  
Dietrich Mack
Keyword(s):  
Foreign Body ◽  
Staphylococcus Epidermidis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Infection Model ◽  
Polysaccharide Intercellular Adhesin ◽  
Wild Type ◽  
Bacterial Strains ◽  
Biofilm Production ◽  
Negative Mutant

ABSTRACT The production of biofilm is thought to be crucial in the pathogenesis of prosthetic-device infections caused byStaphylococcus epidermidis. An experimental animal model was used to assess the importance of biofilm production, which is mediated by polysaccharide intercellular adhesin/hemagglutinin (PIA/HA), in the pathogenesis of a biomaterial-based infection. Mice were inoculated along the length of a subcutaneously implanted intravenous catheter with either wild-type S. epidermidis1457 or its isogenic PIA/HA-negative mutant. The wild-type strain was significantly more likely to cause a subcutaneous abscess than the mutant strain (P < 0.01) and was significantly less likely to be eradicated from the inoculation site by host defense (P < 0.05). In addition, the wild-type strain was found to adhere to the implanted catheters more abundantly than the PIA/HA-negative mutant (P < 0.05). The reliability of the adherence assay was assessed by scanning electron microscopy. To exclude contamination or spontaneous infection, bacterial strains recovered from the experimental animals were compared to inoculation strains by analysis of restriction fragment length polymorphism patterns by pulsed-field gel electrophoresis. In vitro binding of the wild-type strain and its isogenic mutant to a fibronectin-coated surface was similar. These results confirm the importance of biofilm production, mediated by PIA/HA, in the pathogenesis of S. epidermidis experimental foreign body infection.

scholarly journals Role of RegM, a Homologue of the Catabolite Repressor Protein CcpA, in the Virulence of Streptococcus pneumoniae

2002 ◽  
Vol 70 (10) ◽  
pp. 5454-5461 ◽  
Author(s):  
Philippe Giammarinaro ◽  
James C. Paton
Keyword(s):  
Streptococcus Pneumoniae ◽  
Growth Rates ◽  
Type Strain ◽  
Wild Type Strain ◽  
Capsular Polysaccharide ◽  
Ex Vivo ◽  
Wild Type ◽  
Significant Similarity

ABSTRACT As part of a study of virulence gene regulation in Streptococcus pneumoniae, we have identified a gene encoding a homologue of the staphylococcal catabolite control protein CcpA in the pneumococcal genome sequence. The pneumococcal protein, designated RegM, has significant similarity to members of the LacI/GalR family of bacterial regulatory proteins. S. pneumoniae D39 derivatives with insertion-duplication or deletion mutations in regM were significantly attenuated in virulence with respect to the wild-type strain. In defined media containing either sucrose or lactose as sole carbon sources, the in vitro growth rates of D39 and the regM mutants were essentially the same. However, in the presence of galactose the regM mutants grew significantly faster than the wild-type strain, whereas growth rates were significantly lower in the presence of glucose or maltose. These data are consistent with the involvement of regM in the catabolism of carbohydrates in S. pneumoniae. RegM was a repressor of both α-glucosidase and β-galactosidase activities in S. pneumoniae, but unlike the situation in certain other bacteria, it does not mediate the repression of these enzymes by glucose. The observed attenuation in virulence was not attributable to poorer growth of the regM mutants in mouse blood ex vivo, but nevertheless, the mutants were rapidly cleared from the blood of infected mice in vivo. The regM mutation had no apparent impact on expression of several confirmed pneumococcal virulence proteins, but studies employing a lacZ transcriptional fusion construct indicated that mutation of regM resulted in a significant reduction in transcription of the capsular polysaccharide biosynthesis locus (cps). Thus, regM is the first gene outside of the cps locus to be implicated in regulation of capsular gene expression.

scholarly journals Requirement of the galU Gene for Polysaccharide Production by and Pathogenicity and Growth In Planta of Xanthomonas citri subsp. citri

2010 ◽  
Vol 76 (7) ◽  
pp. 2234-2242 ◽  
Author(s):  
Yinping Guo ◽  
Uma Shankar Sagaram ◽  
Jeong-soon Kim ◽  
Nian Wang
Keyword(s):  
Biofilm Formation ◽  
Type Strain ◽  
Virulence Genes ◽  
Wild Type Strain ◽  
Capsular Polysaccharide ◽  
Extracellular Polysaccharides ◽  
Wild Type ◽  
In Planta ◽  
Intercellular Spaces ◽  
Xanthomonas Citri

ABSTRACT Xanthomonas citri subsp. citri is the causal agent of citrus canker, which has a significant impact on citrus production. In this study, we characterized the galU gene of X. citri subsp. citri. Two galU mutants (F6 and D12) were identified in an X. citri subsp. citri EZ-Tn5 <R6Kγori/KAN-2> Tnp transposon library. Rescue cloning, sequence analysis, and Southern blot analysis indicated that both of these mutants had a single copy of the EZ-Tn5 transposon inserted in galU in the chromosome. Further study showed that galU was required for biosynthesis of extracellular polysaccharides (EPS; xanthan gum) and capsular polysaccharide (CPS) and biofilm formation. Mutation of galU resulted in a loss of pathogenicity for grapefruit. The loss of pathogenicity of a galU mutant resulted from its inability to grow in planta rather than from the effect on virulence genes. Quantitative reverse transcription-PCR assays indicated that mutation of galU did not impair the expression of key virulence genes, such as pthA of X. citri subsp. citri. Although D12 had a growth rate similar to that of the wild-type strain in nutrient broth, no D12 population became established in the intercellular spaces of citrus leaves. Coinoculation of a galU mutant with the wild-type strain did not promote growth of the galU mutant in planta. Defects in EPS and CPS production, pathogenicity, and growth in planta of the galU mutant were complemented to the wild-type level using plasmid pCGU2.1 containing an intact galU gene. These data indicate that the galU gene contributes to X. citri subsp. citri growth in intercellular spaces and is involved in EPS and CPS synthesis and biofilm formation.

scholarly journals Mutational Analysis of the Carboxy-Terminal (YGX)4 Repeat Domain of CpsD, an Autophosphorylating Tyrosine Kinase Required for Capsule Biosynthesis in Streptococcus pneumoniae

2003 ◽  
Vol 185 (10) ◽  
pp. 3009-3019 ◽  
Author(s):  
Judy K. Morona ◽  
Renato Morona ◽  
David C. Miller ◽  
James C. Paton
Keyword(s):  
Streptococcus Pneumoniae ◽  
Tyrosine Kinase ◽  
Type Strain ◽  
Wild Type Strain ◽  
Capsular Polysaccharide ◽  
Wild Type ◽  
Protein Tyrosine ◽  
Tyrosine Residues ◽  
Repeat Domain ◽  
Carboxy Terminal

ABSTRACT In Streptococcus pneumoniae, CpsB, CpsC, and CpsD are essential for encapsulation, and mutants containing deletions of cpsB, cpsC, or cpsD exhibit rough colony morphologies. CpsD is an autophosphorylating protein-tyrosine kinase, CpsC is required for CpsD tyrosine phosphorylation, and CpsB is a phosphotyrosine-protein phosphatase. We have previously shown that autophosphorylation of CpsD at tyrosine attenuates its activity and consequently reduces the level of encapsulation and negatively regulates CPS production. In this study, we further investigated the role of the carboxy-terminal (YGX)4 repeat domain of CpsD in encapsulation. A CpsD truncation mutant in which the entire (YGX)4 repeat domain was removed was indistinguishable from a strain in which the entire cpsD gene had been deleted, indicating that the carboxy-terminal (YGX)4 tail is required for CpsD activity in capsular polysaccharide production. Double mutants having a single tyrosine residue at position 2, 3, or 4 in the (YGX)4 repeat domain and lacking CpsB exhibited a rough colony morphology, indicating that in the absence of an active protein-tyrosine phosphatase, phosphorylation of just one of the tyrosine residues in the (YGX)4 repeat was sufficient to inactivate CpsD. When various mutants in which CpsD had either one or combinations of two or three tyrosine residues in the (YGX)4 repeat domain were examined, only those with three tyrosine residues in the (YGX)4 repeat domain were indistinguishable from the wild-type strain. The mutants with either one or two tyrosine residues exhibited mucoid colony morphologies. Further analysis of the mucoid strains indicated that the mucoid phenotype was not due to overproduction of capsular polysaccharide, as these strains actually produced less capsular polysaccharide than the wild-type strain. Thus, the tyrosine residues in the (YGX)4 repeat domain are essential for normal functioning of CpsD.

scholarly journals Use of an Intergenic Region in Pseudomonas syringae pv. Syringae B728a for Site-Directed Genomic Marking of Bacterial Strains for Field Experiments

2001 ◽  
Vol 67 (8) ◽  
pp. 3735-3738 ◽  
Author(s):  
Susan S. Hirano ◽  
David K. Willis ◽  
Murray K. Clayton ◽  
Christen D. Upper
Keyword(s):  
Pseudomonas Syringae ◽  
Intergenic Region ◽  
Type Strain ◽  
Field Experiments ◽  
Wild Type Strain ◽  
Brown Spot ◽  
Wild Type ◽  
Bacterial Strains ◽  
Snap Bean ◽  
Bean Plants

ABSTRACT To construct differentially-marked derivatives of our model wild-type strain, Pseudomonas syringae pv. syringae B728a (a causal agent of bacterial brown spot disease in snap bean plants), for field experiments, we selected a site in the gacS-cysMintergenic region for site-directed insertion of antibiotic resistance marker cassettes. In each of three field experiments, population sizes of the site-directed chromosomally marked B728a derivatives in association with snap bean plants were not significantly different from that of the wild-type strain. Inserts of up to 7 kb of DNA in the intergenic region did not measurably affect fitness of B728a in the field. The site is useful for site-directed genomic insertions of single copies of genes of interest.

scholarly journals Effects of Mutations of RAD50, RAD51, RAD52, and Related Genes on Illegitimate Recombination in Saccharomyces cerevisiae

Genetics ◽  
1996 ◽  
Vol 142 (2) ◽  
pp. 383-391 ◽  
Author(s):  
Yasumasa Tsukamoto ◽  
Jun-ichi Kato ◽  
Hideo Ikeda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Quantitative Analysis ◽  
Structural Analysis ◽  
Recombination Rate ◽  
Type Strain ◽  
Negative Selection ◽  
Wild Type Strain ◽  
Illegitimate Recombination ◽  
Wild Type ◽  
In The Wild

Abstract To examine the mechanism of illegitimate recombination in Saccharomyces cerevisiae, we have developed a plasmid system for quantitative analysis of deletion formation. A can1 cyh2 cell carrying two negative selection markers, the CAN1 and CYH2 genes, on a YCp plasmid is sensitive to canavanine and cycloheximide, but the cell becomes resistant to both drugs when the plasmid has a deletion over the CAN1 and CYH2 genes. Structural analysis of the recombinant plasmids obtained from the resistant cells showed that the plasmids had deletions at various sites of the CAN1-CYH2 region and there were only short regions of homology (1-5 bp) at the recombination junctions. The results indicated that the deletion detected in this system were formed by illegitimate recombination. Study on the effect of several rad mutations showed that the recombination rate was reduced by 30-, 10-, 10-, and 10-fold in the rad52, rad50, mre11, and xrs2 mutants, respectively, while in the rud51, 54, 55, and 57 mutants, the rate was comparable to that in the wild-type strain. The rad52 mutation did not affect length of homology at junction sites of illegitimate recombination.

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