Crystal structure of GAPDH of Streptococcus agalactiae and characterization of its interaction with extracellular matrix molecules

Nagarajan, Revathi; Sankar, Sreejanani; Ponnuraj, Karthe

doi:10.1016/j.micpath.2018.12.020

Cited by 8 publications

(7 citation statements)

References 78 publications

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“…There are many studies that document the binding of bacterial GAPHD to ECM host components. Although most of these studies merely identify one or more of several host binding proteins, only a few studies characterized the binding mechanisms or key residues in the GAPDH structure involved in the interaction (Gründel et al, 2016;Grimmer and Dumke, 2019;Nagarajan et al, 2019). As the spectrum of tested proteins varies between the studies and the binding affinities are not provided in most cases it is impossible to compare the GAPDH binding characteristics across all bacteria.…”

Section: Interaction With Host Targetsmentioning

confidence: 99%

“…M. tuberculosis GAPDH thus acts as dual receptor for both transferrin and lactoferrin. The ability of surface-localized GAPDH to bind transferrin has newly been demonstrated for Streptococcus agalactiae (Nagarajan et al, 2019). Controversial data were published regarding the transferrin-binding cell wall GAPDH in Staphylococcus ssp.…”

Section: Interaction With Host Targetsmentioning

confidence: 99%

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Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality?

Kopeckova

Pávková

Stulı́k

2020

Front. Cell. Infect. Microbiol.

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Bacterial proteins exhibiting two or more unrelated functions, referred to as moonlighting proteins, are suggested to contribute to full virulence manifestation in pathogens. An expanding number of published studies have revealed the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to be a multitasking protein with virulence impact in a number of pathogenic bacteria. This protein can be detected on the bacterial surface or outside the bacterial cell, where it interacts with host proteins. In this way, GAPDH is able to modulate various pathogenic processes. Moreover, it has been shown to be involved in non-enzymatic processes inside the bacterial cell. In this mini review, we summarize main findings concerning the multiple localization and protein interactions of GAPDH derived from bacterial pathogens of humans. We also briefly discuss problems associated with using GAPDH as a vaccine antigen and endeavor to inspire further research to fill gaps in the existing knowledge.

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Section: Interaction With Host Targetsmentioning

confidence: 99%

Section: Interaction With Host Targetsmentioning

confidence: 99%

Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality?

Kopeckova

Pávková

Stulı́k

2020

Front. Cell. Infect. Microbiol.

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“…Previous studies have demonstrated that terminal or internal lysine residues in a number of bacterial Plg receptors are required for optimal interactions with Plg ( Bergmann et al., 2001 ; Derbise et al., 2004 ; Wiles et al., 2010 ; Moreau et al., 2017 ; Nagarajan et al., 2019 ). In view of the ability of L-lysine to inhibit interactions between the MK-rich domain and Plg, as shown above, we hypothesized that LBS in the Plg molecule interact with one or more of the lysine residues that are abundantly present in the MK-rich domain.…”

Section: Resultsmentioning

confidence: 99%

“…Data are means ± SD from three independent experiments conducted in duplicate. Moreau et al, 2017;Nagarajan et al, 2019). For these reasons we hypothesized that one or more of the lysine residues of this domain mediated such interactions.…”

Section: Discussionmentioning

confidence: 99%

Lysine Residues in the MK-Rich Region Are Not Required for Binding of the PbsP Protein From Group B Streptococci to Plasminogen

Coppolino

Romeo

Pietrocola

et al. 2021

Front. Cell. Infect. Microbiol.

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Binding to plasminogen (Plg) enables bacteria to associate with and invade host tissues. The cell wall protein PbsP significantly contributes to the ability of group B streptococci, a frequent cause of invasive infection, to bind Plg. Here we sought to identify the molecular regions involved in the interactions between Plg and PbsP. The K4 Kringle domain of the Plg molecule was required for binding of Plg to whole PbsP and to a PbsP fragment encompassing a region rich in methionine and lysine (MK-rich domain). These interactions were inhibited by free L-lysine, indicating the involvement of lysine binding sites in the Plg molecule. However, mutation to alanine of all lysine residues in the MK-rich domain did not decrease its ability to bind Plg. Collectively, our data identify a novel bacterial sequence that can interact with lysine binding sites in the Plg molecule. Notably, such binding did not require the presence of lysine or other positively charged amino acids in the bacterial receptor. These data may be useful for developing alternative therapeutic strategies aimed at blocking interactions between group B streptococci and Plg.

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“…Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a well-known house-keeping protein, which has been made up by NAD + binding domain (N-terminal) and a catalytic domain (C-terminal)(Nagarajan et al, 2019). The catalytic domain also has an "S-loop" that makes interaction to the NAD + coenzyme of adacent subunit and is considered to work cooperatively(Ayna, 2016).…”

mentioning

confidence: 99%

Structure-Function Analysis Glyceraldehyde-3-Phosphate Dehydrogenase Homologue GapB in Staphylococcus aureus

Almehmadi

2020

International Journal of Nature and Life Sciences

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is the most studied reference protein that catalysis the inter-conversion reaction of glyceraldehyde-3-phosphate into 1,3-diphosphoglycerate using NAD+ as coenzyme. GAPDH is also recognized as an important player in DNA repair mechanisms, autophagic and apoptotic cell deaths and posttranslational modifications. Staphylococcus aureus is Gram positive commensal pathogenic bacteria. In the genome of S. aureus, GapA was assumed to be a glycolytic GAPDH and GapB was assumed to be a gluconeogenic GAPDH. The crystal structure of GapA has already been in preceding studies. However, to my knowledge, no structural studies on the gapB homologue is available in the literature. The main aims of this study were to analyze physicochemical properties and generate a homology model structure of GAPDH homologue GapB in S. aureus. This was carried out by Protparam tool, Phyre2 homology modeling server and PSIPRED secondary structure analysis tool. ProtParam predicted that GapB is a stable and liposoluble protein. Homology modeling studies revealed that each subunit of GapB was made up by two domains: the NAD coenzyme binding-domain and the catalytic domain. The NAD binding domain was shown to contain a Rossman fold. On the other hand, the catalytic domain was made up by a mixture of eight strands of beta sheet and seven alfa helices. PSIPRED analysis revealed that the secondary structure of the GapB contains α-helices (29.91%), extended strands (24.63%) and random coil (45.45%).

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Crystal structure of GAPDH of Streptococcus agalactiae and characterization of its interaction with extracellular matrix molecules

Cited by 8 publications

References 78 publications

Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality?

Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality?

Lysine Residues in the MK-Rich Region Are Not Required for Binding of the PbsP Protein From Group B Streptococci to Plasminogen

Structure-Function Analysis Glyceraldehyde-3-Phosphate Dehydrogenase Homologue GapB in Staphylococcus aureus

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