Variation in the Presence of Neuraminidase Genes among
            <i>Streptococcus pneumoniae</i>
            Isolates with Identical Sequence Types

Pettigrew, Melinda M.; Fennie, Kristopher; York, Matthew P.; Daniels, J.; Ghaffar, Faryal

doi:10.1128/iai.01442-05

Cited by 112 publications

(128 citation statements)

References 45 publications

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“…sing high collagen-binding rates (TLJ11-2, TLJ85-4, TLJ137-4 and TLJ9-1) ( A lack of correlation between serotypes and STs has been demonstrated in many bacterial species, such as Streptococcus pneumoniae, Neisseria meningitidis and Streptococcus agalactiae, and the horizontal transfer of capsular biosynthesis genes related to serotyping is speculated to be the reason (Coffey et al, 1991;Luan et al, 2005;Pettigrew et al, 2006;Swartley et al, 1997). In fact, we also reported the association of one ST with two serotypes in our previous work (Lapirattanakul et al, 2008;Nakano et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Multilocus sequence typing analysis of Streptococcus mutans strains with the cnm gene encoding collagen-binding adhesin

Lapirattanakul

Nakano

Nomura

et al. 2011

Journal of Medical Microbiology

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Streptococcus mutans is one of the oral pathogens associated with infective endocarditis (IE).With respect to bacterial binding ability to the extracellular matrix, the Cnm protein, a cell surface collagen-binding adhesin of S. mutans, is known as one of the possible virulence factors with regard to IE. In this study, we aimed to determine the distribution of the cnm gene, which encodes Cnm, in a large number of clinical isolates of S. mutans from Thai subjects. Then, the cnm-positive strains were classified using a multilocus sequence typing (MLST) scheme, which we constructed previously. In addition, the data were analysed together with our previous MLST data of cnmpositive strains from Japan and Finland in order to evaluate the clonal relationship among S. mutans strains harbouring the cnm gene. The cnm gene was detected in 12.4 % of all 750 Thai isolates, and serotype f showed the highest rate of detection (54.5 %). According to the MLST data, two clonal complex groups were revealed as the important clones related to cnm-positive S. mutans from various origins of isolation. Moreover, the collagen-binding properties of S. mutans strains with the cnm gene were significantly greater than those of strains without the gene, although four cnm-negative strains classified into two sequence types (STs), ST110 and ST136, showed extremely high collagen-binding rates suggesting the presence of additional genes involved with collagen binding in these STs. Taken together, these results provided information on both epidemiological as well as evolutional aspects of S. mutans possessing the cnm gene. INTRODUCTIONStreptococcus mutans is a well-known pathogen of dental caries (Hamada & Slade, 1980), which consists of four serotypes, c, e, f and k (Linzer et al., 1986;). The detection rate of serotype c is highest among the strains isolated from oral cavities, followed by serotype e, while serotypes f and k are regarded as being present in minor proportions . Various pieces of evidence show the association of S. mutans with some life-threatening diseases such as infective endocarditis (IE), although the major species related to IE belong to the mitis group of oral streptococci (Banas, 2004;Mylonakis & Calderwood, 2001). Moreover, continuous detections of this bacterium in specimens from patients suffering from such disease emphasize the importance of S. mutans in IE (Gauduchon et al., 2001;Nomura et al., 2006;Vose et al., 1987;Ullman et al., 1988). Indeed, studies to clarify specific components involved in IE in S. mutans have also been performed worldwide (Beg et al., 2002;Jung et al., 2009; MatsumotoNakano et al., 2009;Miller-Torbert et al., 2008).IE is initiated by the binding of bacterial surface molecules to host extracellular matrix (ECM) proteins exposed on damaged heart tissue (Moreillon & Que, 2004). In S. mutans, collagen-binding adhesin or Cnm protein, encoded by the cnm gene, was reported as a strain-specific collagen-binding molecule (Sato et al., 2004). The Cnm protein possesses a collagen-binding domain (CBD) in ...

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Section: Discussionmentioning

confidence: 99%

Multilocus sequence typing analysis of Streptococcus mutans strains with the cnm gene encoding collagen-binding adhesin

Lapirattanakul

Nakano

Nomura

et al. 2011

Journal of Medical Microbiology

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“…Neuraminidase activity of different pneumococcal isolates can differ greatly [30], for various reasons, such as the presence of one to three different neuraminidase genes [22] and NanA mosaicism that can influence enzyme activity [75]. Regardless of the underlying molecular mechanism, our study provides evidence that neuraminidase activity across a range of different pneumococcal isolates can be antagonized by the combination of α-NanA and α-NanBC mAbs in vitro and in vivo .…”

Section: Discussionmentioning

confidence: 89%

“…Detection of nanA, nanB and nanC gene fragments (~ 500 bp) was performed by PCR as described previously [22]. Neuraminidase genes (~ 3000 bp) were amplified using primers 31R and 31S [57] ( nanA ), B_seq1 and B_seq8 ( nanB ), or C_seq1 and C_seq8 ( nanC ); genes encoding pneumolysin (Ply) and PspA clade defining regions as described elsewhere [58–60].…”

Section: Methodsmentioning

confidence: 99%

“…Neuraminidases (sialidases) are key enzymes in sugar acquisition. Three pneumococcal neuraminidases, NanA, NanB and NanC have been described [19–21], with reported gene frequencies of 100, 96 and 36–51% among clinical isolates, respectively [22,23]. Neuraminidases share critical sequence features, such as the N-terminal signal peptide, a carbohydrate binding module (CBM40) that recognizes sialic acid (lectin-binding domain), and a six-bladed β-propeller catalytic domain (sialidase domain) with an inserted domain of unknown function [24,25].…”

Section: Introductionmentioning

confidence: 99%

“…Although the presence of nanC has initially been suggested to be linked to S. pneumoniae isolates from cerebrospinal fluid [22], this finding could not be confirmed in a more recent study [47]. In addition, pneumococcal isolates harbouring nanC have been implicated to be involved in necrotizing pneumonia and subsequent development of haemolytic uremic syndrome (HUS) [48], a finding that could not be confirmed by another group [49].…”

Section: Introductionmentioning

confidence: 99%

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Assessing the function of pneumococcal neuraminidases NanA, NanB and NanC inin vitroandin vivolung infection models using monoclonal antibodies

et al. 2018

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Streptococcus pneumoniae isolates express up to three neuraminidases (sialidases), NanA, NanB and NanC, all of which cleave the terminal sialic acid of glycan-structures that decorate host cell surfaces. Most research has focused on the role of NanA with limited investigations evaluating the roles of all three neuraminidases in host-pathogen interactions. We generated two highly potent monoclonal antibodies (mAbs), one that blocks the enzymatic activity of NanA and one cross-neutralizing NanB and NanC. Total neuraminidase activity of clinical S. pneumoniae isolates could be inhibited by this mAb combination in enzymatic assays. To detect desialylation of cell surfaces by pneumococcal neuraminidases, primary human tracheal/bronchial mucocilial epithelial tissues were infected with S. pneumoniae and stained with peanut lectin. Simultaneous targeting of the neuraminidases was required to prevent desialylation, suggesting that inhibition of NanA alone is not sufficient to preserve terminal lung glycans. Importantly, we also found that all three neuraminidases increased the interaction of S. pneumoniae with human airway epithelial cells. Lectin-staining of lung tissues of mice pre-treated with mAbs before intranasal challenge with S. pneumoniae confirmed that both anti-NanA and anti-NanBC mAbs were required to effectively block desialylation of the respiratory epithelium in vivo. Despite this, no effect on survival, reduction in pulmonary bacterial load, or significant changes in cytokine responses were observed. This suggests that neuraminidases have no pivotal role in this murine pneumonia model that is induced by high bacterial challenge inocula and does not progress from colonization as it happens in the human host.

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Glycan‐metabolizing enzymes in microbe–host interactions: the Streptococcus pneumoniae paradigm

2018

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Streptococcus pneumoniae is a frequent colonizer of the upper airways; however, it is also an accomplished pathogen capable of causing life-threatening diseases. To colonize and cause invasive disease, this bacterium relies on a complex array of factors to mediate the host-bacterium interaction. The respiratory tract is rich in functionally important glycoconjugates that display a vast range of glycans, and, thus, a key component of the pneumococcus-host interaction involves an arsenal of bacterial carbohydrate-active enzymes to depolymerize these glycans and carbohydrate transporters to import the products. Through the destruction of host glycans, the glycan-specific metabolic machinery deployed by S. pneumoniae plays a variety of roles in the host-pathogen interaction. Here, we review the processing and metabolism of the major host-derived glycans, including N- and O-linked glycans, Lewis and blood group antigens, proteoglycans, and glycogen, as well as some dietary glycans. We discuss the role of these metabolic pathways in the S. pneumoniae-host interaction, speculate on the potential of key enzymes within these pathways as therapeutic targets, and relate S. pneumoniae as a model system to glycan processing in other microbial pathogens.

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Variation in the Presence of Neuraminidase Genes among Streptococcus pneumoniae Isolates with Identical Sequence Types

Cited by 112 publications

References 45 publications

Multilocus sequence typing analysis of Streptococcus mutans strains with the cnm gene encoding collagen-binding adhesin

Multilocus sequence typing analysis of Streptococcus mutans strains with the cnm gene encoding collagen-binding adhesin

Assessing the function of pneumococcal neuraminidases NanA, NanB and NanC inin vitroandin vivolung infection models using monoclonal antibodies

Glycan‐metabolizing enzymes in microbe–host interactions: the Streptococcus pneumoniae paradigm

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