Identification and Molecular Cloning of a Unique Hyaluronan Synthase from Pasteurella multocida

DeAngelis, Paul L.; Wei, Jing; Drake, Richard; Achyuthan, Ann Mary

doi:10.1074/jbc.273.14.8454

Cited by 137 publications

(100 citation statements)

References 25 publications

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“…Gram-negative Carter type A P. multocida possess a HA synthase, pmHAS, that is very distinct at the protein level from the vertebrate and streptococcal HASs (DeAngelis et al, 1998). Furthermore, their intrinsic enzymatic activities also differ: only pmHAS will elongate exogenous HA acceptor oligosaccharides.…”

Section: Evolution Of Gag Synthases Of Bacterial Pathogensmentioning

confidence: 99%

Evolution of glycosaminoglycans and their glycosyltransferases: Implications for the extracellular matrices of animals and the capsules of pathogenic bacteria

DeAngelis

2002

Anat. Rec.

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Glycosaminoglycans (linear polysaccharides with a repeating disaccharide backbone containing an amino sugar) are essential components of extracellular matrices of animals. These complex molecules play important structural, adhesion, and signaling roles in mammals. Direct detection of glycosaminoglycans has been reported in a variety of organisms, but perhaps more definitive tests for the glycosyltransferase genes should be utilized to clarify the distribution of glycosaminoglycans in metazoans. Recently, glycosyltransferases that form the hyaluronan, heparin/heparan, or chondroitin backbone were identified at the molecular level. The three types of glycosyltransferases appear to have evolved independently based on sequence comparisons and other characteristics. All metazoans appear to possess heparin/heparan. Chondroitin is found in some worms, arthropods, and higher animals. Hyaluronan is found only in two of the three main branches of chordates. The presence of several types of glycosaminoglycans in the body allows multiple communication channels and adhesion systems to operate simultaneously. Certain pathogenic bacteria produce extracellular coatings, called capsules, which are composed of glycosaminoglycans that increase their virulence during infection. The capsule helps shield the microbe from the host defenses and/or modulates host physiology. The bacterial and animal polysaccharides are chemically identical or at least very similar. Therefore, no immune response is generated, in contrast to the vast majority of capsular polymers from other bacteria. In microbial systems, it appears that in most cases functional convergent evolution of glycosaminoglycan glycosyltransferases occurred, rather than direct horizontal gene transfer from their vertebrate hosts. Anat Rec 268: 317-326, 2002.

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Section: Evolution Of Gag Synthases Of Bacterial Pathogensmentioning

confidence: 99%

Evolution of glycosaminoglycans and their glycosyltransferases: Implications for the extracellular matrices of animals and the capsules of pathogenic bacteria

DeAngelis

2002

Anat. Rec.

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“…Hyaluronan is widely diffused in nature: it is present in humans, animals -such as, rabbits, bovines, roosters-, bacteria -such as Streptococcus equi, Streptococcus zooepidermicus, Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, Pasteurella multocida- [49,[80][81][82], algae -such as the green algae Chlorella sp. infected by the Chlorovirus [49,83]-, yeasts such as Cryptococcus neoformans- [49] and molluscs [84].…”

Section: Ha Occurrence In Living Organism and Diffusion In Human Bodymentioning

confidence: 99%

Hyaluronic Acid in the 3<sup>rd</sup> Millennium

Fallacara¹,

Baldini²,

Manfredini³

et al. 2018

Preprint

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Since its first isolation in 1934, hyaluronic acid (HA) has been studied across a variety of research areas. This unbranched glycosaminoglycan consisting of repeating disaccharide units of N-acetyl-D-glucosamine and D-glucuronic acid is almost ubiquitary in humans and in other vertebrates. HA is involved in many key processes -including cell signaling, wound reparation, tissue regeneration, morphogenesis, matrix organization and pathobiology-, and has unique physico-chemical properties -such as biocompatibility, biodegradability, mucoadhesivity, hygroscopicity and viscoelasticity. For these reasons, exogenous HA has been investigated as drug delivery system and treatment in cancer, ophthalmology, arthrology, pneumology, rhinology, urology, aesthetic medicine and cosmetic. To improve and customize its properties and applications, HA can be subjected to chemical modifications: conjugation and crosslinking. The present review gives an overview regarding HA, describing its history, physico-chemical, structural and hydrodynamic properties, and biology -occurrence, biosynthesis (by hyaluronan synthases), degradation (by hyaluronidases and oxidative stress), roles, mechanisms of action and receptors. Furthermore, both conventional and recently emerging methods developed for the industrial production of HA and its chemical derivatization are presented. Finally, the medical, pharmaceutical and cosmetic applications of HA and its derivatives are reviewed, reporting examples of HA-based products which currently are on the market or are undergoing further investigations.

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“…The construction and the use of the full-length PmHAS expression plasmid for studies in E. coli were described [3].…”

Section: Production Of Recombinant Full-length Pmhas Proteinsmentioning

confidence: 99%

“…The microbial HA synthases, SpHAS of Group A Streptococcus pyogenes and PmHAS of Type A Pasteurella multocida, are responsible for the polymerization of HA of the extracellular capsule [2,3]. A Xenopus laevis (African clawed frog) protein, XlHAS1, originally called DG42, was the first vertebrate HA synthase to be cloned as an abundant transcript during gastrulation, but at the time its function was not known [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

The functional molecular mass of the Pasteurella hyaluronan synthase is a monomer

Pummill¹,

Kane²,

Kempner

et al. 2007

Biochimica et Biophysica Acta (BBA) - General Subjects

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Hyaluronan (HA), a linear polysaccharide composed of β1,3-GlcNAc-β1,4-GlcUA repeats, is found in the extracellular matrix of vertebrate tissues as well as the capsule of several pathogenic bacteria. All known HA synthases (HASs) are dual-action glycosyltransferases that catalyze the addition of two different sugars from UDP-linked precursors to the growing HA chain. The bacterial hyaluronan synthase, PmHAS from Gram-negative Pasteurella multocida, is a 972-residue membraneassociated protein. Previously, the Gram-positive Streptococcus pyogenes enzyme, SpHAS (419 residues), and the vertebrate enzyme, XlHAS1 (588 residues), were found to function as monomers of protein, but the PmHAS is not similar at the protein sequence level and has quite different enzymological properties. We have utilized radiation inactivation to measure the target size of recombinant full-length and truncated PmHAS. The target size of HAS activity was confirmed using internal enzyme standards of known molecular weight. We found that the Pasteurella HA synthase protein functions catalytically as a monomer. Functional truncated soluble PmHAS also behaves as a polypeptide monomer as assessed by gel filtration chromatography and light scattering.

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Identification and Molecular Cloning of a Unique Hyaluronan Synthase from Pasteurella multocida

Cited by 137 publications

References 25 publications

Evolution of glycosaminoglycans and their glycosyltransferases: Implications for the extracellular matrices of animals and the capsules of pathogenic bacteria

Evolution of glycosaminoglycans and their glycosyltransferases: Implications for the extracellular matrices of animals and the capsules of pathogenic bacteria

Hyaluronic Acid in the 3<sup>rd</sup> Millennium

The functional molecular mass of the Pasteurella hyaluronan synthase is a monomer

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