The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions

Modun, Belinda; Morrissey, Julie A.; Williams, Paul

doi:10.1016/s0966-842x(00)01728-5

Cited by 90 publications

(54 citation statements)

References 34 publications

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“…Cell surface-associated glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) of S. epidermidis, S. pyogenes, S. pneumoniae, and Candida albicans have been reported (4,17,20,49). On S. epidermidis, GAPDH was found to act as a transferrin-binding protein on the cell surface (42,43). In S. pyogenes, GAPDH on the cell surface binds fibronectin, lysozyme, and the cytoskeletal proteins myosin and actin (49).…”

Section: Discussionmentioning

confidence: 99%

Contribution of the Mannan Backbone of Cryptococcal Glucuronoxylomannan and a Glycolytic Enzyme ofStaphylococcus aureusto Contact-Mediated Killing ofCryptococcus neoformans

et al. 2007

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The fungal pathogen Cryptococcus neoformans is killed by the bacterium Staphylococcus aureus, and the killing is inhibited by soluble capsular polysaccharides. To investigate the mechanism of killing, cells in coculture were examined by scanning and transmission electron microscopy. S. aureus attached to the capsule of C. neoformans, and the ultrastructure of the attached C. neoformans cells was characteristic of dead cells. To identify the molecules that contributed to the fungal-bacterial interaction, we treated each with NaIO 4 or protease. Treatment of C. neoformans with NaIO 4 promoted adherence. It was inferred that cleavage of xylose and glucuronic acid side chains of glucuronoxylomannan (GXM) allowed S. aureus to recognize mannose residues in the backbone, which resisted periodate oxidation. On the other hand, treatment of S. aureus with protease decreased adherence, suggesting that protein contributed to attachment in S. aureus. In confirmation, side chain-cleaved polysaccharide or defined ␣-(133)-mannan inhibited the killing at lower concentrations than native GXM did. Also, these polysaccharides reduced the adherence of the two species and induced clumping of pure S. aureus cells. ␣-(133)-Mannooligosaccharides with a degree of polymerization (DP) of >3 induced cluster formation of S. aureus in a dose-dependent manner. Surface plasmon resonance analyses showed interaction of GXM and surface protein from S. aureus; the interaction was inhibited by oligosaccharides with a DP of >3. Conformations of ␣-(133) oligosaccharides were predicted. The three-dimensional structures of mannooligosaccharides larger than triose appeared curved and could be imagined to be recognized by a hypothetical staphylococcal lectin. Native polyacrylamide gel electrophoresis of staphylococcal protein followed by electroblotting, enzyme-linked immunolectin assay, protein staining, and N-terminal amino acid sequencing suggested that the candidate protein was triosephosphate isomerase (TPI). The enzymatic activities were confirmed by using whole cells of S. aureus. TPI point mutants of S. aureus decreased the ability to interact with C. neoformans. Thus, TPI on S. aureus adheres to the capsule of C. neoformans by recognizing the structure of mannotriose units in the backbone of GXM; we suggest that this contact is required for killing of C. neoformans.

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Section: Discussionmentioning

confidence: 99%

Contribution of the Mannan Backbone of Cryptococcal Glucuronoxylomannan and a Glycolytic Enzyme ofStaphylococcus aureusto Contact-Mediated Killing ofCryptococcus neoformans

et al. 2007

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“…The inability of the bacteria to grow at low initial densities in the presence of partially saturated transferrin suggests that iron displacement from transferrin requires high bacterial density. It has been suggested that diphosphoglycerate, whose formation is catalysed by the transferrin receptor glyceraldehyde-3-phosphate dehydrogenase, may facilitate iron removal from the receptor-bound transferrin [13]. Diphosphoglycerate and other organic phosphates were previously shown to displace iron from transferrin at millimolar concentrations [22].…”

Section: Discussionmentioning

confidence: 99%

Dependence of Staphylococcus epidermidis on non-transferrin-bound iron for growth

Matinaho

2001

FEMS Microbiology Letters

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The ability of Staphylococcus epidermidis strains to grow in the presence of human transferrin and varying amounts of ferric iron was studied. At initial bacterial densities up to 10 4 cfu ml 31 , none of the three strains grew when transferrin iron saturation was below the full saturation point, whereas the bacteria grew consistently when transferrin was fully iron-saturated and there was non-transferrin-bound iron in the medium. Precultivation of the bacteria under iron-restricted conditions to induce siderophore production did not abolish the growth dependence on non-transferrin-bound iron. At initial bacterial densities of 10 6 cfu ml 31 , the bacteria proliferated consistently also in the presence of partially saturated transferrin. The results indicate that at low bacterial densities, S. epidermidis cannot utilise transferrin-bound iron for growth and that its proliferation is dependent on non-transferrin-bound iron. ß

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“…iron-saturated transferrin) and lactoferrin (also known as lactotransferrin) on the surface of a diverse range of cell types, including macrophages, and upon iron starvation many cells prefer to use surfacelocalized GAPDH for holotransferrin uptake rather than TfR1 Modun et al, 1998;Modun et al, 2000;Raje et al, 2007;Rawat et al, 2012). Recently, we have also demonstrated that cells enhance their secretion of GAPDH into the extracellular milieu (sGAPDH) when they are depleted of iron.…”

Section: Introductionmentioning

confidence: 99%

Moonlighting cell surface GAPDH recruits Apo Transferrin to effect iron egress from mammalian cells

Sheokand

Malhotra

Kumar

et al. 2014

Journal of Cell Science

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The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions

Cited by 90 publications

References 34 publications

Contribution of the Mannan Backbone of Cryptococcal Glucuronoxylomannan and a Glycolytic Enzyme ofStaphylococcus aureusto Contact-Mediated Killing ofCryptococcus neoformans

Contribution of the Mannan Backbone of Cryptococcal Glucuronoxylomannan and a Glycolytic Enzyme ofStaphylococcus aureusto Contact-Mediated Killing ofCryptococcus neoformans

Dependence of Staphylococcus epidermidis on non-transferrin-bound iron for growth

Moonlighting cell surface GAPDH recruits Apo Transferrin to effect iron egress from mammalian cells

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