Clostridial hydrolytic enzymes degrading extracellular components

Matsushita, Osamu; Okabe, Akinobu

doi:10.1016/s0041-0101(01)00163-5

Cited by 100 publications

(78 citation statements)

References 75 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Most bacterial sialidases preferentially cleave α-(2-3)-linked sialic acids, and are found in species that live in close contact with vertebrate host cells as commensals or facultative pathogens. Sialidase activity is involved in bacterial colonization and dissemination, ECM degradation, and induced host-cell death [12,20,21,22,23]. It has also been proposed that bacterial desialylation of host glycoconjugates could expose or form new host antigens to play a role in autoimmune complications of infection [24,25].…”

Section: Introductionmentioning

confidence: 99%

Genetic variation in sialidase and linkage to N-acetylneuraminate catabolism in Mycoplasma synoviae

May

Brown

2008

Microbial Pathogenesis

View full text Add to dashboard Cite

We explored the genetic basis for intraspecific variation in mycoplasmal sialidase activity that correlates with virulence, and its potentially advantageous linkage to nutrient catabolism. Polymorphism in N-acetylneuraminate scavenging and degradation genes (sialidase, Nacetylneuraminate lyase, N-acetylmannosamine kinase, N-acetylmannosamine-6-phosphate epimerase, N-acetylglucosamine-6-phosphate deacetylase, and glucosamine-6-phosphate deaminase) was evident among eight strains of the avian pathogen Mycoplasma synoviae. Most differences were single nucleotide polymorphisms, ranging from 0.34 ± 0.04 substitutions per 100 bp for N-acetylmannosamine kinase to 0.65 ± 0.03 for the single-copy sialidase gene nanI. Missense mutations were twice as common as silent mutations in nanI; 26% resulted in amino acids dissimilar to consensus; and there was a 12-base deletion near the nanI promoter in strain WVU1853 T , supporting a complex genetic basis for differences in sialidase activity. Two strains had identical frameshifts in the N-acetylneuraminate lyase gene nanA, resulting in nonsense mutations, and both had downstream deletions in nanA. Such genetic lesions uncouple extracellular liberation of sialic acid from generation of fructose-6-phosphate and pyruvate via intracellular N-acetylneuraminate degradation. Retention of nanI by such strains, but not others in the M. synoviae phylogenetic cluster, is evidence that sialidase has an important non-nutritional role in the ecology of M. synoviae and certain other mycoplasmas.

show abstract

Section: Introductionmentioning

confidence: 99%

Genetic variation in sialidase and linkage to N-acetylneuraminate catabolism in Mycoplasma synoviae

May

Brown

2008

Microbial Pathogenesis

View full text Add to dashboard Cite

show abstract

“…They are involved in recognition processes, connection with ECM components, and intercellular interactions (1 (2,36,42,48). Deprotected polymers promote further enzymatic degradation of the ECM to release potential bacterial nutrients (26,38). As predicted from the presence of nanI, the M. alligatoris genome also encodes a sialic acid lyase (nanA; GenBank accession number AY515696), which has not been found in any other mycoplasma characterized to date, that could catalyze the release of pyruvate from sialic acid, liberating N-acetylglucosamine for entry into glycolysis as described above.…”

Section: Discussionmentioning

confidence: 99%

“…The predicted M. alligatoris NanI homolog was 511 amino acids long and exhibited 30% amino acid identity and 47% amino acid similarity to C. perfringens NanI excluding the C. perfringens leader sequence, which sequence alignment and PSORT analyses showed was absent in M. alligatoris (signal score, Ϫ4.29). The signature YRIP motif and four SXDXGXTW Asp box motifs, as well as the catalytic R-37, D-62, D-100, and E-230 residues of C. perfringens NanI (26,40), were conserved in M. alligatoris. The M. alligatoris NanI homolog was interspersed with eight putative UGA W codons but no other W codons.…”

Section: Genomicsmentioning

confidence: 99%

“…The severity of the lesions correlates with the numbers of M. alligatoris cells in affected tissues, suggesting that a spreading factor(s) contributes to the virulence. The extracellular matrix (ECM)-degrading enzymes that act as bacterial spreading factors include hyaluronidases, sialidases, and mucinases (26). In this report we describe the use of comparative genomics to guide the discovery of a hyaluronidase and a novel sialidase which are potential virulence factors of M. alligatoris.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Spreading Factors of Mycoplasma alligatoris , a Flesh-Eating Mycoplasma

Brown¹,

Zacher²,

Farmerie

2004

J Bacteriol

View full text Add to dashboard Cite

Mycoplasma alligatoris causes lethal invasive disease of alligators and caimans. A homolog of the nagH gene, encoding a hyaluronidase secreted by Clostridium perfringens, and a C. perfringens hyaluronidase nagI or nagK pseudogene were discovered in the M. alligatoris genome. The nagH gene was detected by PCR in the closest relative of M. alligatoris, Mycoplasma crocodyli, but not in 40 other species representing the Mycoplasma hominis, Mycoplasma pneumoniae, and Spiroplasma phylogenetic clusters. The hyaluronidase activity in the cellular fraction of M. alligatoris and M. crocodyli SP4 broth cultures was equivalent to 10 ؊16 U of Streptomyces hyalurolyticus hyaluronidase CFU ؊1 . Negligible activity was present in the cell-free supernatant fraction. No chondroitinase activity was detected. There is also a novel homolog of the nanI gene, which encodes a sialidase secreted by C. perfringens, in the M. alligatoris genome. The signature YRIP and SXDXGXTW motifs and catalytic residues of the clostridial sialidase are conserved in the mycoplasmal gene, but the leader sequence necessary for its secretion by C. perfringens is absent. The gene was not detected by PCR in any other mycoplasma. Potent cell-associated sialidase activity was present in M. alligatoris colonies on agar but not in the cell-free supernatants of broth cultures or in M. crocodyli. The presence of hyaluronidase and sialidase in M. alligatoris is consistent with the rapid invasiveness and necrotizing effects of this organism, and the lack of sialidase in M. crocodyli is consistent with its comparatively attenuated virulence. This genetic and biochemical evidence suggests that the spreading factors hyaluronidase and sialidase, a combination unprecedented in mycoplasmas, are the basis of the virulence of M. alligatoris.Mycoplasma alligatoris causes a lethal invasive disease in adult alligators (Alligator mississippiensis) and closely related caimans (Caiman latirostris). The pathology observed as early as 1 week after infection by instillation via the glottis includes necrotizing pneumonia, severe pericarditis, necrotizing myocarditis, lymphocytic interstitial nephritis, lymphocytic periportal hepatitis, splenic hyperplasia, pyogranulomatous meningitis, and necrotizing synovitis (9,10,11,13,18,33). Hatchling alligators also rapidly developed disseminated M. alligatoris mycoplasmosis after intratracheal instillation, and the lesions are similar to those of adults and include acute multifocal brainstem hemorrhage (35). Mycoplasma crocodyli (23), the closest known relative of M. alligatoris (98% 16S rRNA gene similarity [9]), causes a similar necrotizing synovitis and occasionally subacute pneumonia in Nile crocodiles (Crocodylus niloticus) (27,28). The severity of the lesions correlates with the numbers of M. alligatoris cells in affected tissues, suggesting that a spreading factor(s) contributes to the virulence. The extracellular matrix (ECM)-degrading enzymes that act as bacterial spreading factors include hyaluronidases, sialidases, and mucinases (26...

show abstract

“…HA is a multifunctional, nonsulfated, high-molecularweight polysaccharide found throughout the animal kingdom, especially in the extracellular matrix of soft connective tissues (1)(2)(3). The key role of the HA-HAase system has been recognized in a number of pathophysiological processes such as embryogenesis, angiogenesis, inflammation, disease progression, wound healing, microbial infection, and the diffusion of systemic toxins/venoms (3)(4)(5). Several studies have confirmed that the altered HAase activity was observed in liver cirrhosis, liver fibrosis, diabetes, osteoarthritis, transplantation, and tumor progression (3,6,7).…”

mentioning

confidence: 99%

Effect of anticoagulants on the plasma hyaluronidase activities

Sharma

Mahadeswaraswamy

Kumar

et al. 2009

Clinical Laboratory Analysis

View full text Add to dashboard Cite

Mammalian hyaluronidases (HAases) are an endo‐β‐N‐acetyl‐hexosaminidases that degrade hyaluronan (HA) and have been implicated in diverse pathophysiological functions. Several pathological conditions, such as diabetes, monoclonal gammapathy, and bladder and prostate tumors, report the distorted plasma HAase activity. However, the plasma HAase (hHyal‐1) activity has been presumed to change with the circulating HA level and serves as an early marker for several diseases. It has been generally practised to use the anticoagulants such as tri‐sodium citrate/di‐sodium EDTA/heparin for the preparation of plasma for both biochemical and clinical analyses. In the present investigation, theeffect of anticoagulants on plasma HAaseactivity was evaluated and compared with the serum HAase activity that is devoid of anticoagulants as no study provides information in this regard. The results suggested that the plasma HAase activity in the presence of the recommended concentration of EDTA was highly comparable/similar to that of the serum HAase activity. In contrast, citrated or heparinized plasma recorded a significantly reduced level of activity than that of the serum HAase activity. In conclusion, our results suggested that the EDTA‐treated plasma samples are a better choice compared with heparin and citrated samples to assess the HAase activity. J. Clin. Lab. Anal. 23:29–33, 2009. © 2009 Wiley‐Liss, Inc.

show abstract

Clostridial hydrolytic enzymes degrading extracellular components

Cited by 100 publications

References 75 publications

Genetic variation in sialidase and linkage to N-acetylneuraminate catabolism in Mycoplasma synoviae

Genetic variation in sialidase and linkage to N-acetylneuraminate catabolism in Mycoplasma synoviae

Spreading Factors of Mycoplasma alligatoris , a Flesh-Eating Mycoplasma

Effect of anticoagulants on the plasma hyaluronidase activities

Contact Info

Product

Resources

About