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Article ; Online: Mycobacterium tuberculosis H37Rv enolase (Rv1023)- expression, characterization and effect of host dependent modifications on protein functionality

Kumar, Ajay / Boradia, Vishant Mahendra / Mahajan, Apurwa / Kumaran, S. / Raje, Manoj / Raje, Chaaya Iyengar

Biochimie. 2023 Nov., v. 214 p.102-113

2023

Abstract: Mycobacterium tuberculosis enolase is an essential glycolytic enzyme that catalyzes the conversion of 2, phosphoglycerate (PGA) to phosphoenol pyruvate (PEP). It is also a crucial link between glycolysis and the tricarboxylic acid (TCA) pathway. The ... ...

Abstract	Mycobacterium tuberculosis enolase is an essential glycolytic enzyme that catalyzes the conversion of 2, phosphoglycerate (PGA) to phosphoenol pyruvate (PEP). It is also a crucial link between glycolysis and the tricarboxylic acid (TCA) pathway. The depletion of PEP has recently been associated with the emergence of non-replicating drug resistant bacteria. Enolase is also known to exhibit multiple alternate functions, such as promoting tissue invasion via its role as a plasminogen (Plg) receptor. In addition, proteomic studies have identified the presence of enolase in the Mtb degradosome and in biofilms. However, the precise role in these processes has not been elaborated. The enzyme was recently identified as a target for 2-amino thiazoles - a novel class of anti-mycobacterials. In vitro assays and characterization of this enzyme were unsuccessful due to the inability to obtain functional recombinant protein. In the present study, we report the expression and characterization of enolase using Mtb H37Ra as a host strain. Our study demonstrates that the enzyme activity and alternate functions of this protein are significantly impacted by the choice of expression host (Mtb H37Ra or E. coli). Detailed analysis of the protein from each source revealed subtle differences in the post-translational modifications. Lastly, our study confirms the role of enolase in Mtb biofilm formation and describes the potential for inhibiting this process.
Keywords	Escherichia coli ; Mycobacterium tuberculosis ; biofilm ; drug resistance ; enzyme activity ; glycolysis ; phosphopyruvate hydratase ; plasminogen ; proteomics ; pyruvic acid ; recombinant proteins ; thiazoles ; Enolase ; Protein expression ; Protein multifunctionality
Language	English
Dates of publication	2023-11
Size	p. 102-113.
Publishing place	Elsevier B.V.
Document type	Article ; Online
ZDB-ID	120345-9
ISSN	0300-9084
ISSN	0300-9084
DOI	10.1016/j.biochi.2023.06.012
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Chronic hyperglycemia impairs anti-microbial function of macrophages in response to Mycobacterium tuberculosis infection.

Chaubey, Gaurav Kumar / Modanwal, Radheshyam / Dilawari, Rahul / Talukdar, Sharmila / Dhiman, Asmita / Chaudhary, Surbhi / Patidar, Anil / Raje, Chaaya Iyengar / Raje, Manoj

Immunologic research

2024

Abstract: Diabetes mellitus (DM) is a major risk factor for tuberculosis (TB), though the underlying mechanisms linking DM and TB remain ambiguous. Macrophages are a key player in the innate immune response and their phagocytic ability is enhanced in response to ... ...

Abstract	Diabetes mellitus (DM) is a major risk factor for tuberculosis (TB), though the underlying mechanisms linking DM and TB remain ambiguous. Macrophages are a key player in the innate immune response and their phagocytic ability is enhanced in response to microbial infections. Upon infection or inflammation, they also repel invading pathogens by generating; reactive oxygen species (ROS), reactive nitrogen species (RNS), pro-inflammatory cytokines (IL-1β and IL-6), and anti-inflammatory cytokines (IL-10). However, the robustness of these innate defensive capabilities of macrophages when exposed to hyperglycemia remains unclear. In our current work, we explored the production of these host defense molecules in response to challenge with Mycobacterium tuberculosis (Mtb) infection and lipopolysaccharide (LPS) stimulation. Utilizing peritoneal macrophages from high-fat diet + streptozotocin induced diabetic mice and hyperglycemic THP-1-derived macrophages as model systems; we found that LPS stimulation and Mtb infection were ineffective in stimulating the production of ROS, RNS, and pro-inflammatory cytokines in cells exposed to hyperglycemia. On the contrary, an increase in production of anti-inflammatory cytokines was observed. To confirm the mechanism of decreased anti-bacterial activity of the diabetic macrophage, we explored activation status of these compromised macrophages and found decreased surface expression of activation (TLR-4) and differentiation markers (CD11b and CD11c). We postulate that this could be the cause for higher susceptibility for Mtb infection among diabetic individuals.
Language	English
Publishing date	2024-02-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	632857-x
ISSN	1559-0755 ; 0257-277X
ISSN (online)	1559-0755
ISSN	0257-277X
DOI	10.1007/s12026-024-09462-z
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Article ; Online: Glyceraldehyde-3-Phosphate Dehydrogenase Binds with Spike Protein and Inhibits the Entry of SARS-CoV-2 into Host Cells.

Dilawari, Rahul / Chaubey, Gaurav Kumar / Modanwal, Radheshyam / Dhiman, Asmita / Talukdar, Sharmila / Kumar, Ajay / Raje, Chaaya Iyengar / Raje, Manoj

Journal of innate immunity

2024 Volume 16, Issue 1, Page(s) 133–142

Abstract: Introduction: Coronavirus disease 2019 caused by coronavirus-2 (SARS-CoV-2) has emerged as an aggressive viral pandemic. Health care providers confront a challenging task for rapid development of effective strategies to combat this and its long-term ... ...

Abstract	Introduction: Coronavirus disease 2019 caused by coronavirus-2 (SARS-CoV-2) has emerged as an aggressive viral pandemic. Health care providers confront a challenging task for rapid development of effective strategies to combat this and its long-term after effects. Virus entry into host cells involves interaction between receptor-binding domain (RBD) of spike (S) protein S1 subunit with angiotensin converting enzyme present on host cells. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a moonlighting enzyme involved in cellular glycolytic energy metabolism and micronutrient homeostasis. It is deployed in various cellular compartments and the extra cellular milieu. Though it is known to moonlight as a component of mammalian innate immune defense machinery, till date its role in viral restriction remains unknown. Method: Recombinant S protein, the RBD, and human GAPDH protein were used for solid phase binding assays and biolayer interferometry. Pseudovirus particles expressing four different strain variants of S protein all harboring ZsGreen gene as marker of infection were used for flow cytometry-based infectivity assays. Results: Pseudovirus entry into target cells in culture was significantly inhibited by addition of human GAPDH into the extracellular medium. Binding assays demonstrated that human GAPDH binds to S protein and RBD of SARS-CoV-2 with nanomolar affinity. Conclusions: Our investigations suggest that this interaction of GAPDH interferes in the viral docking with hACE2 receptors, thereby affecting viral ingress into mammalian cells.
MeSH term(s)	Humans ; Spike Glycoprotein, Coronavirus/metabolism ; SARS-CoV-2/physiology ; COVID-19/virology ; Protein Binding ; Virus Internalization ; HEK293 Cells ; Betacoronavirus/physiology ; Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism ; Pneumonia, Viral/virology ; Pneumonia, Viral/immunology ; Pandemics ; Coronavirus Infections/virology ; Angiotensin-Converting Enzyme 2/metabolism ; Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)
Chemical Substances	Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Glyceraldehyde-3-Phosphate Dehydrogenases (EC 1.2.1.-) ; GAPDH protein, human (EC 1.2.1.12) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; ACE2 protein, human (EC 3.4.17.23) ; Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (EC 1.2.1.12)
Language	English
Publishing date	2024-02-07
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; News
ZDB-ID	2454158-8
ISSN	1662-8128 ; 1662-811X
ISSN (online)	1662-8128
ISSN	1662-811X
DOI	10.1159/000535634
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Article ; Online: Mycobacterium tuberculosis H37Rv enolase (Rv1023)- expression, characterization and effect of host dependent modifications on protein functionality.

Kumar, Ajay / Boradia, Vishant Mahendra / Mahajan, Apurwa / Kumaran, S / Raje, Manoj / Raje, Chaaya Iyengar

Biochimie

2023 Volume 214, Issue Pt B, Page(s) 102–113

Abstract	Mycobacterium tuberculosis enolase is an essential glycolytic enzyme that catalyzes the conversion of 2, phosphoglycerate (PGA) to phosphoenol pyruvate (PEP). It is also a crucial link between glycolysis and the tricarboxylic acid (TCA) pathway. The depletion of PEP has recently been associated with the emergence of non-replicating drug resistant bacteria. Enolase is also known to exhibit multiple alternate functions, such as promoting tissue invasion via its role as a plasminogen (Plg) receptor. In addition, proteomic studies have identified the presence of enolase in the Mtb degradosome and in biofilms. However, the precise role in these processes has not been elaborated. The enzyme was recently identified as a target for 2-amino thiazoles - a novel class of anti-mycobacterials. In vitro assays and characterization of this enzyme were unsuccessful due to the inability to obtain functional recombinant protein. In the present study, we report the expression and characterization of enolase using Mtb H37Ra as a host strain. Our study demonstrates that the enzyme activity and alternate functions of this protein are significantly impacted by the choice of expression host (Mtb H37Ra or E. coli). Detailed analysis of the protein from each source revealed subtle differences in the post-translational modifications. Lastly, our study confirms the role of enolase in Mtb biofilm formation and describes the potential for inhibiting this process.
MeSH term(s)	Mycobacterium tuberculosis ; Phosphopyruvate Hydratase/genetics ; Phosphopyruvate Hydratase/metabolism ; Escherichia coli/metabolism ; Proteomics ; Plasminogen/metabolism
Chemical Substances	Phosphopyruvate Hydratase (EC 4.2.1.11) ; Plasminogen (9001-91-6)
Language	English
Publishing date	2023-06-27
Publishing country	France
Document type	Journal Article
ZDB-ID	120345-9
ISSN	1638-6183 ; 0300-9084
ISSN (online)	1638-6183
ISSN	0300-9084
DOI	10.1016/j.biochi.2023.06.012
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Article ; Online: Excess iron aggravates the severity of COVID-19 infection.

Chaubey, Gaurav Kumar / Dilawari, Rahul / Modanwal, Radheshyam / Talukdar, Sharmila / Dhiman, Asmita / Raje, Chaaya Iyengar / Raje, Manoj

Free radical biology & medicine

2023 Volume 208, Page(s) 186–193

Abstract: Coronavirus disease-19 (COVID-19) can induce severe inflammation of the lungs and respiratory system. Severe COVID-19 is frequently associated with hyper inflammation and hyper-ferritinemia. High iron levels are known to trigger pro-inflammatory effects. ...

Abstract	Coronavirus disease-19 (COVID-19) can induce severe inflammation of the lungs and respiratory system. Severe COVID-19 is frequently associated with hyper inflammation and hyper-ferritinemia. High iron levels are known to trigger pro-inflammatory effects. Cumulative iron loading negatively impacts on a patients innate immune effector functions and increases the risk for infection related complications. Prognosis of severe acute respiratory SARS-CoV-2 patients may be impacted by iron excess. Iron is an essential co-factor for numerous essential cellular enzymes and vital cellular operations. Viruses hijack cells in order to replicate, and efficient replication requires an iron-replete host. Utilizing iron loaded cells in culture we evaluated their susceptibility to infection by pseudovirus expressing the SARS-CoV-2 spike protein and resultant cellular inflammatory response. We observed that, high levels of iron enhanced host cell ACE2 receptor expression contributing to higher infectivity of pseudovirus. In vitro Cellular iron overload also synergistically enhanced the levels of; reactive oxygen species, reactive nitrogen species, pro-inflammatory cytokines (IL-1β, IL-6, IL-8 & TNF-α) and chemokine (CXCL-1&CCL-4) production in response to inflammatory stimulation of cells with spike protein. These results were confirmed using an in vivo mouse model. In future, limiting iron levels may be a promising adjuvant strategy in treating viral infection.
MeSH term(s)	Humans ; Animals ; Mice ; COVID-19 ; SARS-CoV-2 ; Inflammation ; Iron Overload ; Iron
Chemical Substances	spike protein, SARS-CoV-2 ; Iron (E1UOL152H7)
Language	English
Publishing date	2023-08-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2023.08.011
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Zs.A 2109: Show issues

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Article ; Online: Host glyceraldehyde-3-phosphate dehydrogenase-mediated iron acquisition is hijacked by intraphagosomal Mycobacterium tuberculosis

Patidar, Anil / Malhotra, Himanshu / Chaudhary, Surbhi / Kumar, Manoj / Dilawari, Rahul / Chaubey, Gaurav Kumar / Dhiman, Asmita / Modanwal, Radheshyam / Talukdar, Sharmila / Raje, Chaaya Iyengar / Raje, Manoj

Cell. Mol. Life Sci.. 2022 Jan., v. 79, no. 1 p.62-62

2022

Abstract: Availability of iron is a key factor in the survival and multiplication of Mycobacterium tuberculosis (M.tb) within host macrophage phagosomes. Despite host cell iron regulatory machineries attempts to deny supply of this essential micronutrient, ... ...

Abstract	Availability of iron is a key factor in the survival and multiplication of Mycobacterium tuberculosis (M.tb) within host macrophage phagosomes. Despite host cell iron regulatory machineries attempts to deny supply of this essential micronutrient, intraphagosomal M.tb continues to access extracellular iron. In the current study, we report that intracellular M.tb exploits mammalian secreted Glyceraldehyde 3-phosphate dehydrogenase (sGAPDH) for the delivery of host iron carrier proteins lactoferrin (Lf) and transferrin (Tf). Studying the trafficking of iron carriers in infected cells we observed that sGAPDH along with the iron carrier proteins are preferentially internalized into infected cells and trafficked to M.tb containing phagosomes where they are internalized by resident mycobacteria resulting in iron delivery. Collectively our findings provide a new mechanism of iron acquisition by M.tb involving the hijack of host sGAPDH. This may contribute to its successful pathogenesis and provide an option for targeted therapeutic intervention.
Keywords	Mycobacterium tuberculosis ; glyceraldehyde 3-phosphate ; glyceraldehyde-3-phosphate dehydrogenase ; iron ; lactoferrin ; macrophages ; mammals ; pathogenesis ; phagosomes ; therapeutics ; transferrin
Language	English
Dates of publication	2022-01
Size	p. 62.
Publishing place	Springer International Publishing
Document type	Article ; Online
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-021-04110-3
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Article ; Online: Characterization of the enzymatic and multifunctional properties of Acinetobacter baumannii erythrose-4-phosphate dehydrogenase (E4PDH).

Nimma, Ramesh / Kumar, Ajay / Gani, Zahid / Gahlawat, Anuj / Dilawari, Rahul / Rohilla, Rajesh Kumar / Kumbhar, Hemangi / Garg, Prabha / Chopra, Sidharth / Raje, Manoj / Iyengar Raje, Chaaya

Microbial pathogenesis

2023 Volume 175, Page(s) 105992

Abstract: Infections due to Acinetobacter baumannii (A. baumannii) are rapidly increasing worldwide and consequently therapeutic options for treatment are limited. The emergence of multi drug resistant (MDR) strains has rendered available antibiotics ineffective, ... ...

Abstract	Infections due to Acinetobacter baumannii (A. baumannii) are rapidly increasing worldwide and consequently therapeutic options for treatment are limited. The emergence of multi drug resistant (MDR) strains has rendered available antibiotics ineffective, necessitating the urgent discovery of new drugs and drug targets. The vitamin B6 biosynthetic pathway has been considered as a potential antibacterial drug target but it is as yet uncharacterized for A. baumannii. In the current work, we have carried out in silico and biochemical characterization of Erythrose-4-phosphate dehydrogenase (E4PDH) (EC 1.2.1.72). This enzyme catalyzes the first step in the deoxyxylulose-5-phosphate (DXP) dependent Vitamin B6 biosynthetic pathway i.e. the conversion of d-erythrose-4-phosphate (E4P) to 4-Phosphoerythronate. E4PDH also possesses an additional activity whereby it can catalyze the conversion of Glyceraldehyde-3-phosphate (G3P) to 1,3 bisphosphoglycerate (1,3BPG). Our studies have revealed that this enzyme exhibits an alternate moonlighting function as a cell surface receptor for the human iron transport proteins transferrin (Tf) and lactoferrin (Lf). The present work reports the internalization of Tf and consequent iron acquisition as an alternate strategy for iron acquisition. Given its essential role in two crucial pathways i.e. metabolism and iron acquisition, A. baumannii E4PDH may play a vital role in bacterial pathogenesis.
MeSH term(s)	Humans ; Acinetobacter baumannii ; Anti-Bacterial Agents/pharmacology ; Iron/metabolism ; Vitamin B 6 ; Oxidoreductases ; Phosphates/pharmacology ; Drug Resistance, Multiple, Bacterial
Chemical Substances	erythrose (X3EI0WE8Q4) ; Anti-Bacterial Agents ; Iron (E1UOL152H7) ; Vitamin B 6 (8059-24-3) ; Oxidoreductases (EC 1.-) ; Phosphates
Language	English
Publishing date	2023-01-14
Publishing country	England
Document type	Journal Article
ZDB-ID	632772-2
ISSN	1096-1208 ; 0882-4010
ISSN (online)	1096-1208
ISSN	0882-4010
DOI	10.1016/j.micpath.2023.105992
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Article ; Online: Regulation of Macrophage Cell Surface GAPDH Alters LL-37 Internalization and Downstream Effects in the Cell.

Dhiman, Asmita / Talukdar, Sharmila / Chaubey, Gaurav Kumar / Dilawari, Rahul / Modanwal, Radheshyam / Chaudhary, Surbhi / Patidar, Anil / Boradia, Vishant Mahendra / Kumbhar, Pradeep / Raje, Chaaya Iyengar / Raje, Manoj

Journal of innate immunity

2023 Volume 15, Issue 1, Page(s) 581–598

Abstract: Mycobacterium tuberculosis (M.tb), the major causative agent of tuberculosis, has evolved mechanisms to evade host defenses and persist within host cells. Host-directed therapies against infected cells are emerging as an effective option. Cationic host ... ...

Abstract	Mycobacterium tuberculosis (M.tb), the major causative agent of tuberculosis, has evolved mechanisms to evade host defenses and persist within host cells. Host-directed therapies against infected cells are emerging as an effective option. Cationic host defense peptide LL-37 is known to internalize into cells and induce autophagy resulting in intracellular killing of M.tb. This peptide also regulates the immune system and interacts with the multifunctional protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) inside macrophages. Our investigations revealed that GAPDH moonlights as a mononuclear cell surface receptor that internalizes LL-37. We confirmed that the surface levels of purinergic receptor 7, the receptor previously reported for this peptide, remained unaltered on M.tb infected macrophages. Upon infection or cellular activation with IFNγ, surface recruited GAPDH bound to and internalized LL-37 into endocytic compartments via a lipid raft-dependent process. We also discovered a role for GAPDH in LL-37-mediated autophagy induction and clearance of intracellular pathogens. In infected macrophages wherein GAPDH had been knocked down, we observed an inhibition of LL-37-mediated autophagy which was rescued by GAPDH overexpression. This process was dependent on intracellular calcium and p38 MAPK pathways. Our findings reveal a previously unknown process by which macrophages internalize an antimicrobial peptide via cell surface GAPDH and suggest a moonlighting role of GAPDH in regulating cellular phenotypic responses of LL-37 resulting in reduction of M.tb burden.
MeSH term(s)	Humans ; Macrophages ; Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism ; Mycobacterium tuberculosis/physiology ; Tuberculosis ; Antimicrobial Cationic Peptides/metabolism
Chemical Substances	Glyceraldehyde-3-Phosphate Dehydrogenases (EC 1.2.1.-) ; Antimicrobial Cationic Peptides
Language	English
Publishing date	2023-04-20
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2454158-8
ISSN	1662-8128 ; 1662-811X
ISSN (online)	1662-8128
ISSN	1662-811X
DOI	10.1159/000530083
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Article ; Online: Bifunctionalized nanobioprobe based rapid color-shift assay for typhoid targeting Vi capsular polysaccharide.

Choudhary, Megha / Bisht, Bhawana / Saini, Jai Kumar / Bharti / Singh, Pargat / Bhardwaj, Priya / Dilawari, Rahul / Pinnaka, Anil Kumar / Ray, Pallab / Gupta, Madhu / Sethi, Sunil / Suri, C Raman / Raje, Manoj / Bhalla, Vijayender

Biosensors & bioelectronics

2023 Volume 228, Page(s) 115195

Abstract: Typhoid fever is an acute illness caused by Salmonella Typhi and the current diagnostic gap leads to inaccurate, over-diagnosis of typhoid leading to excessive use of antibiotics. Herein, to address the challenges we describe a new rapid color-shift ... ...

Abstract	Typhoid fever is an acute illness caused by Salmonella Typhi and the current diagnostic gap leads to inaccurate, over-diagnosis of typhoid leading to excessive use of antibiotics. Herein, to address the challenges we describe a new rapid color-shift assay based on a novel bifunctional nanobioprobe (Vi-AgNP probe) that is functionalized with specific biomarker Vi polysaccharide and also has the co-presence of Ag as urease inhibitor. The immunoreactions between the Vi with specific antibodies (Abs) present in typhoid patient sample forms a shielding barrier over Vi-AgNP probe rendering the urease to be active, generating colored output. Vi polysaccharide coating on the AgNP was visualized using HRTEM. TEM was performed to get insight into shielding barrier formation by the Abs. MST (microscale thermophoresis) data showed less binding Kd of 7.43 μM in presence of Abs whereas probe with urease showed efficient binding with Kd 437 nM. The assay was validated using 53 human sera samples and proven effective with 100% sensitivity. The assay showed relative standard deviation (RSD) of 4.3% estimated using rabbit anti-Vi Abs. The entire procedure could be completed within 15 min. Unlike lateral flow based assays, our assay does not require multiple combination of Abs for detection. The assay format was also found compatible in paper strip test that provides promising opportunities to develop low-cost on-spot assay for clinical diagnostics.
MeSH term(s)	Animals ; Humans ; Rabbits ; Antibodies, Bacterial ; Biosensing Techniques ; Polysaccharides, Bacterial ; Salmonella typhi ; Typhoid Fever/diagnosis ; Urease
Chemical Substances	Antibodies, Bacterial ; Polysaccharides, Bacterial ; Urease (EC 3.5.1.5)
Language	English
Publishing date	2023-03-08
Publishing country	England
Document type	Journal Article
ZDB-ID	1011023-9
ISSN	1873-4235 ; 0956-5663
ISSN (online)	1873-4235
ISSN	0956-5663
DOI	10.1016/j.bios.2023.115195
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Article ; Online: Exposure of a specific pleioform of multifunctional glyceraldehyde 3-phosphate dehydrogenase initiates CD14-dependent clearance of apoptotic cells.

Chaudhary, Surbhi / Patidar, Anil / Dhiman, Asmita / Chaubey, Gaurav Kumar / Dilawari, Rahul / Talukdar, Sharmila / Modanwal, Radheshyam / Raje, Manoj

Cell death & disease

2021 Volume 12, Issue 10, Page(s) 892

Abstract: Rapid clearance of apoptotic cells by phagocytes is crucial for organogenesis, tissue homeostasis, and resolution of inflammation. This process is initiated by surface exposure of various 'eat me' ligands. Though phosphatidylserine (PS) is the best ... ...

Abstract	Rapid clearance of apoptotic cells by phagocytes is crucial for organogenesis, tissue homeostasis, and resolution of inflammation. This process is initiated by surface exposure of various 'eat me' ligands. Though phosphatidylserine (PS) is the best recognized general recognition ligand till date, recent studies have shown that PS by itself is not sufficient for clearance of apoptotic cells. In this study, we have identified a specific pleioform of GAPDH (Glyceraldehyde 3-phosphate dehydrogenase) that functions as an 'eat me' signal on apoptotic cell surface. This specific form of GAPDH which is exposed on surface of apoptotic cells was found to interact with CD14 present on plasma membrane of phagocytes leading to their engulfment. This is the first study demonstrating the novel interaction between multifunctional GAPDH and the phagocytic receptor CD14 resulting in apoptotic cell clearance (efferocytosis).
MeSH term(s)	Apoptosis ; Cell Line ; Cell Membrane/metabolism ; Exocytosis ; Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism ; Humans ; Lipopolysaccharide Receptors/metabolism ; Lysosomes/metabolism ; Phagocytes/metabolism ; Phagocytosis ; Phosphatidylserines/metabolism ; Phospholipid Transfer Proteins/metabolism ; Protein Binding ; Protein Isoforms/metabolism ; Stress, Physiological
Chemical Substances	Lipopolysaccharide Receptors ; Phosphatidylserines ; Phospholipid Transfer Proteins ; Protein Isoforms ; Glyceraldehyde-3-Phosphate Dehydrogenases (EC 1.2.1.-)
Language	English
Publishing date	2021-09-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-021-04168-8
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