Increased yield of a lysozyme after self-cloning of the gene in Streptomyces coelicolor ?M�ller?

Bräu, Barbara; Hilgenfeld, Rolf; Schlingmann, M.; Marquardt, Rüdiger; Birr, E.; Wohlleben, Wolfgang; Aufderheide, Karin; Pühler, Alfred

doi:10.1007/bf00180575

Cited by 19 publications

(4 citation statements)

References 35 publications

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“…Some experiments carried out by a group of European investigators using the INTOSPACE facilities and the Russian Cosima space carrier were indeterminate according to their report 61,63 although several interesting observations emerged. A number of different proteins were crystallized, in some cases with positive benefit, whereas for others the contrary was true.…”

Section: Initial Results (Proof Of Concept)mentioning

confidence: 99%

Microgravity protein crystallization

McPherson

DeLucas

2015

npj Microgravity

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Over the past 20 years a variety of technological advances in X-ray crystallography have shortened the time required to determine the structures of large macromolecules (i.e., proteins and nucleic acids) from several years to several weeks or days. However, one of the remaining challenges is the ability to produce diffraction-quality crystals suitable for a detailed structural analysis. Although the development of automated crystallization systems combined with protein engineering (site-directed mutagenesis to enhance protein solubility and crystallization) have improved crystallization success rates, there remain hundreds of proteins that either cannot be crystallized or yield crystals of insufficient quality to support X-ray structure determination. In an attempt to address this bottleneck, an international group of scientists has explored use of a microgravity environment to crystallize macromolecules. This paper summarizes the history of this international initiative along with a description of some of the flight hardware systems and crystallization results.

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Section: Initial Results (Proof Of Concept)mentioning

confidence: 99%

Microgravity protein crystallization

McPherson

DeLucas

2015

npj Microgravity

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“…A variety of lysozymes of bacterial origin are also known to exist (Nakimbugwe et al, 2006). Although most are not able to digest staphylococcal peptidoglycan, due to the ability of some staphylococci to O-acetylate their peptidoglycan (Bera et al, 2006), there are other lysozymes that can (Brau et al, 1991). In light of the fact that phage genomes are notoriously recombinogenic, it is difficult to reconcile why there is not a single glycosidase domain among the SH3b containing phage or staphylococcal peptidoglycan hydrolases.…”

Section: Discussionmentioning

confidence: 95%

Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain

Becker¹,

Foster‐Frey²,

Stodola³

et al. 2009

Gene

107

145

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“…Cellosyl (Hoechst AG, Frankfurt, Germany), a muramidase produced by Streptomyces coelicolor (8), catalyzes the breaking of the bond between MurNAc and GlcNAc in the PepG glycan backbone, resulting in disaccharide subunits substituted with peptide side chains. A proportion of these are linked together by PepG cross-bridging (Fig.…”

Section: Methodsmentioning

confidence: 99%

Organ Injury and Cytokine Release Caused by Peptidoglycan Are Dependent on the Structural Integrity of the Glycan Chain

Myhre¹,

Stuestøl²,

Dahle³

et al. 2004

Infect Immun

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Several studies have implicated a role of peptidoglycan (PepG) as a pathogenicity factor in sepsis and organ injury, in part by initiating the release of inflammatory mediators. We wanted to elucidate the structural requirements of PepG to trigger inflammatory responses and organ injury. Injection of native PepG into anesthetized rats caused moderate but significant increases in the levels of alanine aminotransferase, aspartate aminotransferase, ␥-glutamyl transferase, and bilirubin (markers of hepatic injury and/or dysfunction) and creatinine and urea (markers of renal dysfunction) in serum, whereas PepG pretreated with muramidase to digest the glycan backbone failed to do this. In an ex vivo model of human blood, PepG containing different amino acids induced similar levels of the cytokines tumor necrosis factor alpha (TNF-␣), interleukin-6 (IL-6), IL-8, and IL-10, as determined by plasma analyses (enzyme-linked immunosorbent assay). Hydrolysis of the Staphylococcus aureus cross-bridge with lysostaphin resulted in moderately reduced release of TNF-␣, IL-6, IL-8, and IL-10, whereas muramidase digestion nearly abolished the ability to induce cytokine release and IL-6 mRNA accumulation in CD14؉ monocytes compared to intact PepG. However, additional experiments showed that muramidase-treated PepG synergized with lipopolysaccharide to induce TNF-␣ and IL-10 release in whole blood, despite its lack of inflammatory activity when administered alone. Based on these studies, we hypothesize that the structural integrity of the glycan chain of the PepG molecule is very important for the pathogenic effects of PepG. The amino acid composition of PepG, however, does not seem to be essential for the inflammatory properties of the molecule.

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Increased yield of a lysozyme after self-cloning of the gene in Streptomyces coelicolor ?M�ller?

Cited by 19 publications

References 35 publications

Microgravity protein crystallization

Microgravity protein crystallization

Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain

Organ Injury and Cytokine Release Caused by Peptidoglycan Are Dependent on the Structural Integrity of the Glycan Chain

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