Cloning, Sequencing and Expression of a Sialidase Gene from Clostridium sordellii G12

Rothe, Bernd; Roggentin, Peter; Frank, Ronald; Blöcker, Helmut; Schauer, Roland

doi:10.1099/00221287-135-11-3087

Cited by 30 publications

(24 citation statements)

References 30 publications

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“…The scores (in S.D. units) for an alignment of the sequences of G9, the sialidases of Salmonella typhimurium (41), Clostridium perfringens (42), and Clostridium sordellii (43) and the rat and hamster cytosolic sialidases, over the regions indicated, are listed in Table II. These scores provide a good indication that G9 shares a common ancestor with the bacterial sialidases.…”

Section: Resultsmentioning

confidence: 99%

Identification of a Sialidase Encoded in the Human Major Histocompatibility Complex

Milner

Smith

Carrillo

et al. 1997

Journal of Biological Chemistry

101

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Mammalian sialidases are important in modulating the sialic acid content of cell-surface and intracellular glycoproteins. However, the full extent of this enzyme family and the physical and biochemical properties of its individual members are unclear. We have identified a novel gene, G9, in the human major histocompatibility complex (MHC), that encodes a 415-amino acid protein sharing 21-28% sequence identity with the bacterial sialidases and containing three copies of the Asp-block motif characteristic of these enzymes. The level of sequence identity between human G9 and a cytosolic sialidase identified in rat and hamster (28 -29%) is much less than would be expected for analogous proteins in these species, suggesting that G9 is distinct from the cytosolic enzyme. Expression of G9 in insect cells has confirmed that it encodes a sialidase, which shows optimal activity at pH 4.6, but appears to have limited substrate specificity. The G9 protein carries an N-terminal signal sequence and immunofluorescence staining of COS7 cells expressing recombinant G9 shows localization of this sialidase exclusively to the endoplasmic reticulum. The location of the G9 gene, within the human MHC, corresponds to that of the murine Neu-1 locus, suggesting that these are analogous genes. One of the functions attributed to Neu-1 is the up-regulation of sialidase activity during T cell activation.

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Section: Resultsmentioning

confidence: 99%

Identification of a Sialidase Encoded in the Human Major Histocompatibility Complex

Milner

Smith

Carrillo

et al. 1997

Journal of Biological Chemistry

101

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“…Other lipoproteins appear to be released from the bacterial cell depending on the phase of growth (54,55), and lipoprotein enzymes may be released via proteolytic cleavage (50,51,56). Whether the release of lipoproteins from the cell is widely exploited as a mechanism for regulating their activity at the cell surface or is simply a consequence of general cell turnover and lysis is unclear.…”

Section: Discussionmentioning

confidence: 99%

“…Table 1 reveals that a number of enzyme activities such as sialidase (56) and hyaluronate synthetase (37) are associated with putative lipoproteins. A lipoprotein with binding activity for the immunosuppresant FK506 (i.e., an immunophilin), which also possessed peptidyl-prolyl cis-trans isomerase activity, has been identified in Streptomyces chrysomalus (53).…”

Section: Substrate-binding Lipoproteins In Transport Systemsmentioning

confidence: 99%

Lipoproteins of gram-positive bacteria

1995

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“…It is hypothesized that sialidase contributes to the virulence of some pathogenic organisms, especially those that inhabit and invade mucosal surfaces (7). Drzeniek (14) found sialidase activity in bacterial isolates that belong to the orders Pseudomonadales and Eubacteriales, and sialidases have been cloned from Clostridium species (35,36,37), Vibrio cholerae (48), Streptococcus pneumoniae (4, 5), Micromonospora viridifaciens (38), and Salmonella enterica serotype Typhimurium (21). Many of these bacterial sialidases have about 20% similarity at the amino acid level (21).…”

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confidence: 99%

Cloning and Characterization of Sialidases with 2-6′ and 2-3′ Sialyl Lactose Specificity from Pasteurella multocida

et al. 2000

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Pasteurella multocida is a mucosal pathogen that colonizes the respiratory system of susceptible hosts. Most isolates of P. multocida produce sialidase activity, which may contribute to colonization of the respiratory tract or the production of lesions in an active infection. We have cloned and sequenced a sialidase gene, nanH, from a fowl cholera isolate of P. multocida. Sequence analysis of NanH revealed that it exhibited significant amino acid sequence homology with many microbial sialidases. Insertional inactivation of nanH resulted in a mutant strain that was not deficient in sialidase production. However, this mutant exhibited reduced enzyme activity and growth rate on 2-3 sialyl lactose compared to the wild type. Subsequently, we demonstrated the presence of two sialidases by cloning another sialidase gene that differed from nanH in DNA sequence and substrate specificity. NanB demonstrated activity on both 2-3 and 2-6 sialyl lactose, while NanH demonstrated activity only on 2-3 sialyl lactose. Neither enzyme liberated sialic acid from colominic acid (2-8 sialyl lactose). Recombinant E. coli containing the sialidase genes were able to utilize several sialoconjugants when they were provided as sole carbon sources in minimal medium. These data suggest that sialidases have a nutritional function and may contribute to the ability of P. multocida to colonize and persist on vertebrate mucosal surfaces.Pasteurella multocida is a gram-negative coccobacillus of the family Pasteurellaceae and is a normal inhabitant of the upper respiratory system of many animals (24). The organism has a broad host range and is commonly a secondary pathogen in upper respiratory infections. Serotype D virulent isolates are toxigenic, but all serotypes produce capsules which confer serum resistance and resistance to phagocytosis (42). However, it is unusual to isolate a P. multocida strain that does not produce sialidase activity (40). Sialidases (neuraminidases; EC 3.2.1.18) are enzymes that liberate sialic acid from sialylconjugated glycoproteins, glycolipids, or colominic acids by cleaving alphaketosidic linkages. It is hypothesized that sialidase contributes to the virulence of some pathogenic organisms, especially those that inhabit and invade mucosal surfaces (7). Drzeniek (14) found sialidase activity in bacterial isolates that belong to the orders Pseudomonadales and Eubacteriales, and sialidases have been cloned from Clostridium species (35,36,37), Vibrio cholerae (48), Streptococcus pneumoniae (4, 5), Micromonospora viridifaciens (38), and Salmonella enterica serotype Typhimurium (21). Many of these bacterial sialidases have about 20% similarity at the amino acid level (21).Sialidases have been implicated as bacterial virulence factors (7, 34). It has been shown that a sialidase-deficient mutant of S. pneumoniae was less able to colonize and persist on mucosal surfaces than the wild type (46). In addition, a Bacteroides fragilis sialidase-deficient mutant was attenuated in the rat abscess model (18). The role of sialidase in ...

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Cloning, Sequencing and Expression of a Sialidase Gene from Clostridium sordellii G12

Cited by 30 publications

References 30 publications

Identification of a Sialidase Encoded in the Human Major Histocompatibility Complex

Identification of a Sialidase Encoded in the Human Major Histocompatibility Complex

Lipoproteins of gram-positive bacteria

Cloning and Characterization of Sialidases with 2-6′ and 2-3′ Sialyl Lactose Specificity from Pasteurella multocida

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