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Article: Recognition of

Loh, Su Ning / Anthony, Ian Russell / Gavor, Edem / Lim, Xin Shan / Kini, R Manjunatha / Mok, Yu Keung / Sivaraman, J

2024 Volume 13, Issue 1

Abstract: Salivary proteins from mosquitoes have received significant attention lately due to their potential to develop therapeutic treatments or vaccines for mosquito-borne diseases. Here, we report the characterization of LTRIN (lymphotoxin beta receptor ... ...

Abstract	Salivary proteins from mosquitoes have received significant attention lately due to their potential to develop therapeutic treatments or vaccines for mosquito-borne diseases. Here, we report the characterization of LTRIN (lymphotoxin beta receptor inhibitor), a salivary protein known to enhance the pathogenicity of ZIKV by interrupting the LTβR-initiated NF-κB signaling pathway and, therefore, diminish the immune responses. We demonstrated that the truncated C-terminal LTRIN (ΔLTRIN) is a dimeric protein with a stable alpha helix-dominant secondary structure, which possibly aids in withstanding the temperature fluctuations during blood-feeding events. ΔLTRIN possesses two Ca
Language	English
Publishing date	2024-01-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology13010042
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Article ; Online: Structural and functional characterization of Aedes aegypti pupal cuticle protein that controls dengue virus infection.

Huang, Qingqing / Gavor, Edem / Tulsian, Nikhil Kumar / Fan, Jingsong / Lin, Qingsong / Mok, Yu Keung / Kini, R Manjunatha / Sivaraman, J

Protein science : a publication of the Protein Society

2023 Volume 32, Issue 10, Page(s) e4761

Abstract: The pupal cuticle protein from Aedes aegypti (AaPC) inhibits dengue virus (DENV) infection; however, the underlying mechanism of this inhibition remains unknown. Here, we report that AaPC is an intrinsically disordered protein and interacts with domain I/ ...

Abstract	The pupal cuticle protein from Aedes aegypti (AaPC) inhibits dengue virus (DENV) infection; however, the underlying mechanism of this inhibition remains unknown. Here, we report that AaPC is an intrinsically disordered protein and interacts with domain I/II of the DENV envelope protein via residues Asp59, Asp61, Glu71, Asp73, Ser75, and Asp80. AaPC can directly bind to and cause the aggregation of DENV, which in turn blocks virus infection during the virus-cell fusion stage. AaPC may also influence viral recognition and attachment by interacting with human immune receptors DC-SIGN and CD4. These findings enhance our understanding of the role of AaPC in mitigating viral infection and suggest that AaPC is a potential target for developing inhibitors or antibodies to control dengue virus infection.
MeSH term(s)	Animals ; Humans ; Dengue ; Dengue Virus/physiology ; Aedes ; Pupa ; Mosquito Vectors
Language	English
Publishing date	2023-08-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4761
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Structure of Aedes aegypti carboxypeptidase B1-inhibitor complex uncover the disparity between mosquito and non-mosquito insect carboxypeptidase inhibition mechanism.

Gavor, Edem / Choong, Yeu Khai / Jobichen, Chacko / Mok, Yu Keung / Kini, R Manjunatha / Sivaraman, J

Protein science : a publication of the Protein Society

2021 Volume 30, Issue 12, Page(s) 2445–2456

Abstract: Metallocarboxypeptidases (MCPs) in the mosquito midgut play crucial roles in infection, as well as in mosquito dietary digestion, reproduction, and development. MCPs are also part of the digestive system of plant-feeding insects, representing key targets ...

Abstract	Metallocarboxypeptidases (MCPs) in the mosquito midgut play crucial roles in infection, as well as in mosquito dietary digestion, reproduction, and development. MCPs are also part of the digestive system of plant-feeding insects, representing key targets for inhibitor development against mosquitoes/mosquito-borne pathogens or as antifeedant molecules against plant-feeding insects. Notably, some non-mosquito insect B-type MCPs are primarily insensitive to plant protease inhibitors (PPIs) such as the potato carboxypeptidase inhibitor (PCI; MW 4 kDa), an inhibitor explored for cancer treatment and insecticide design. Here, we report the crystal structure of Aedes aegypti carboxypeptidase-B1 (CPBAe1)-PCI complex and compared the binding with that of PCI-insensitive CPBs. We show that PCI accommodation is determined by key differences in the active-site regions of MCPs. In particular, the loop regions α6-α7 (Leu
MeSH term(s)	Aedes/enzymology ; Amino Acid Sequence ; Animals ; Carboxypeptidase B/antagonists & inhibitors ; Carboxypeptidase B/chemistry ; Carboxypeptidase B/genetics ; Carboxypeptidase B/metabolism ; Carboxypeptidases A/antagonists & inhibitors ; Carboxypeptidases A/chemistry ; Carboxypeptidases A/genetics ; Carboxypeptidases A/metabolism ; Catalytic Domain ; Cattle ; Cloning, Molecular ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Insect Proteins/antagonists & inhibitors ; Insect Proteins/chemistry ; Insect Proteins/genetics ; Insect Proteins/metabolism ; Kinetics ; Models, Molecular ; Protease Inhibitors/chemistry ; Protease Inhibitors/pharmacology ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Species Specificity ; Substrate Specificity
Chemical Substances	Insect Proteins ; Protease Inhibitors ; Recombinant Proteins ; Carboxypeptidases A (EC 3.4.17.1) ; Carboxypeptidase B (EC 3.4.17.2)
Language	English
Publishing date	2021-11-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4212
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Identification of Aedes aegypti salivary gland proteins interacting with human immune receptor proteins.

Gavor, Edem / Choong, Yeu Khai / Liu, Yonghao / Pompon, Julien / Ooi, Eng Eong / Mok, Yu Keung / Liu, Haiyan / Kini, R Manjunatha / Sivaraman, J

PLoS neglected tropical diseases

2022 Volume 16, Issue 9, Page(s) e0010743

Abstract: Mosquito saliva proteins modulate the human immune and hemostatic systems and control mosquito-borne pathogenic infections. One mechanism through which mosquito proteins may influence host immunity and hemostasis is their interactions with key human ... ...

Abstract	Mosquito saliva proteins modulate the human immune and hemostatic systems and control mosquito-borne pathogenic infections. One mechanism through which mosquito proteins may influence host immunity and hemostasis is their interactions with key human receptor proteins that may act as receptors for or coordinate attacks against invading pathogens. Here, using pull-down assays and proteomics-based mass spectrometry, we identified 11 Ae. aegypti salivary gland proteins (SGPs) (e.g., apyrase, Ae. aegypti venom allergen-1 [AaVA-1], neutrophil stimulating protein 1 [NeSt1], and D7 proteins), that interact with one or more of five human receptor proteins (cluster of differentiation 4 [CD4], CD14, CD86, dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin [DC-SIGN], and Toll-like receptor 4 [TLR4]). We focused on CD4- and DC-SIGN-interacting proteins and confirmed that CD4 directly interacts with AaVA-1, D7, and NeST1 recombinant proteins and that AaVA-1 showed a moderate interaction with DC-SIGN using ELISA. Bacteria responsive protein 1 (AgBR1), an Ae. aegypti saliva protein reported to enhance ZIKV infection in humans but that was not identified in our pull-down assay moderately interacts with CD4 in the ELISA assay. Functionally, we showed that AaVA-1 and NeST1 proteins promoted activation of CD4+ T cells. We propose the possible impact of these interactions and effects on mosquito-borne viral infections such as dengue, Zika, and chikungunya viruses. Overall, this study provides key insight into the vector-host (protein-protein) interaction network and suggests roles for these interactions in mosquito-borne viral infections.
MeSH term(s)	Aedes ; Allergens ; Animals ; Apyrase ; Humans ; Intercellular Adhesion Molecule-3/metabolism ; Mosquito Vectors ; Recombinant Proteins/metabolism ; Salivary Proteins and Peptides/metabolism ; Toll-Like Receptor 4/metabolism
Chemical Substances	Allergens ; Intercellular Adhesion Molecule-3 ; Recombinant Proteins ; Salivary Proteins and Peptides ; Toll-Like Receptor 4 ; Apyrase (EC 3.6.1.5)
Language	English
Publishing date	2022-09-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2429704-5
ISSN	1935-2735 ; 1935-2735
ISSN (online)	1935-2735
ISSN	1935-2735
DOI	10.1371/journal.pntd.0010743
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Article ; Online: Structural Basis of SARS-CoV-2 and SARS-CoV Antibody Interactions.

Gavor, Edem / Choong, Yeu Khai / Er, Shi Yin / Sivaraman, Hariharan / Sivaraman, J

Trends in immunology

2020 Volume 41, Issue 11, Page(s) 1006–1022

Abstract: The 2019 coronavirus pandemic remains a major public health concern. Neutralizing antibodies (nAbs) represent a cutting-edge antiviral strategy. We focus here on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and SARS-CoV, and discuss ... ...

Abstract	The 2019 coronavirus pandemic remains a major public health concern. Neutralizing antibodies (nAbs) represent a cutting-edge antiviral strategy. We focus here on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and SARS-CoV, and discuss current progress in antibody research against rampant SARS-CoV-2 infections. We provide a perspective on the mechanisms of SARS-CoV-2-derived nAbs, comparing these with existing SARS-CoV-derived antibodies. We offer insight into how these antibodies cross-react and cross-neutralize by analyzing available structures of spike (S) glycoprotein-antibody complexes. We also propose ways of adopting antibody-based strategies - such as cocktail antibody therapeutics against SARS-CoV-2 - to overcome the possible resistance of currently identified mutants and mitigate possible antibody-dependent enhancement (ADE) pathologies. This review provides a platform for the progression of antibody and vaccine design against SARS-CoV-2, and possibly against future coronavirus pandemics.
MeSH term(s)	Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Antibodies, Neutralizing/immunology ; Antibodies, Neutralizing/metabolism ; Antibodies, Viral/immunology ; Antibodies, Viral/metabolism ; Betacoronavirus/immunology ; Betacoronavirus/metabolism ; Betacoronavirus/physiology ; COVID-19 ; COVID-19 Vaccines ; Coronavirus Infections/immunology ; Coronavirus Infections/prevention & control ; Coronavirus Infections/virology ; Humans ; Pandemics/prevention & control ; Pneumonia, Viral/immunology ; Pneumonia, Viral/prevention & control ; Pneumonia, Viral/virology ; Protein Binding ; Severe acute respiratory syndrome-related coronavirus/immunology ; Severe acute respiratory syndrome-related coronavirus/metabolism ; SARS-CoV-2 ; Viral Vaccines/administration & dosage ; Viral Vaccines/immunology
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; Viral Vaccines
Keywords	covid19
Language	English
Publishing date	2020-09-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2036831-8
ISSN	1471-4981 ; 1471-4906
ISSN (online)	1471-4981
ISSN	1471-4906
DOI	10.1016/j.it.2020.09.004
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Article ; Online: Structural Basis of SARS-CoV-2- and SARS-CoV-Receptor Binding and Small-Molecule Blockers as Potential Therapeutics.

Sivaraman, Hariharan / Er, Shi Yin / Choong, Yeu Khai / Gavor, Edem / Sivaraman, J

Annual review of pharmacology and toxicology

2020 Volume 61, Page(s) 465–493

Abstract: Over the past two decades, deadly coronaviruses, with the most recent being the severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) 2019 pandemic, have majorly challenged public health. The path for virus invasion into humans and other ... ...

Abstract	Over the past two decades, deadly coronaviruses, with the most recent being the severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) 2019 pandemic, have majorly challenged public health. The path for virus invasion into humans and other hosts is mediated by host-pathogen interactions, specifically virus-receptor binding. An in-depth understanding of the virus-receptor binding mechanism is a prerequisite for the discovery of vaccines, antibodies, and small-molecule inhibitors that can interrupt this interaction and prevent or cure infection. In this review, we discuss the viral entry mechanism, the known structural aspects of virus-receptor interactions (SARS-CoV-2 S/humanACE2, SARS-CoV S/humanACE2, and MERS-CoV S/humanDPP4), the key protein domains and amino acid residues involved in binding, and the small-molecule inhibitors and other drugs that have (as of June 2020) exhibited therapeutic potential. Specifically, we review the potential clinical utility of two transmembrane serine protease 2 (TMPRSS2)-targeting protease inhibitors, nafamostat mesylate and camostat mesylate, as well as two novel potent fusion inhibitors and the repurposed Ebola drug, remdesivir, which is specific to RNA-dependent RNA polymerase, against human coronaviruses, including SARS-CoV-2.
MeSH term(s)	Angiotensin-Converting Enzyme 2/drug effects ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; COVID-19/drug therapy ; Humans ; Protease Inhibitors/therapeutic use ; Receptors, Virus/drug effects ; Small Molecule Libraries
Chemical Substances	Antiviral Agents ; Protease Inhibitors ; Receptors, Virus ; Small Molecule Libraries ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Keywords	covid19
Language	English
Publishing date	2020-08-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	196587-6
ISSN	1545-4304 ; 0362-1642
ISSN (online)	1545-4304
ISSN	0362-1642
DOI	10.1146/annurev-pharmtox-061220-093932
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Article ; Online: Structural Basis of SARS-CoV-2 and SARS-CoV Antibody Interactions

Gavor, Edem / Choong, Yeu Khai / Er, Shi Yin / Sivaraman, Hariharan / Sivaraman, J.

Trends in Immunology

2020 Volume 41, Issue 11, Page(s) 1006–1022

Keywords	Immunology ; Immunology and Allergy ; covid19
Language	English
Publisher	Elsevier BV
Publishing country	us
Document type	Article ; Online
ZDB-ID	2036831-8
ISSN	1471-4981 ; 1471-4906
ISSN (online)	1471-4981
ISSN	1471-4906
DOI	10.1016/j.it.2020.09.004
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Article ; Online: Structure of

Gavor, Edem / Choong, Yeu Khai / Tulsian, Nikhil Kumar / Nayak, Digant / Idris, Fakhriedzwan / Sivaraman, Hariharan / Ting, Donald Heng Rong / Sylvie, Alonso / Mok, Yu Keung / Kini, R Manjunatha / Sivaraman, J

Life science alliance

2021 Volume 5, Issue 1

Abstract: Metallocarboxypeptidases play critical roles in the development of mosquitoes and influence pathogen/parasite infection of the mosquito midgut. Here, we report the crystal structure ... ...

Abstract	Metallocarboxypeptidases play critical roles in the development of mosquitoes and influence pathogen/parasite infection of the mosquito midgut. Here, we report the crystal structure of
MeSH term(s)	Aedes/enzymology ; Aedes/virology ; Amino Acid Sequence ; Animals ; Binding Sites ; Carboxypeptidase B/chemistry ; Carboxypeptidase B/genetics ; Carboxypeptidase B/metabolism ; Catalytic Domain ; Dengue/prevention & control ; Dengue/transmission ; Dengue/virology ; Dengue Virus/physiology ; Host Microbial Interactions ; Infection Control ; Models, Biological ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Sequence Analysis, DNA ; Structure-Activity Relationship ; Substrate Specificity ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/metabolism
Chemical Substances	Viral Envelope Proteins ; Carboxypeptidase B (EC 3.4.17.2)
Language	English
Publishing date	2021-11-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.202101211
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Article: Structural Basis of SARS-CoV-2 and SARS-CoV Antibody Interactions

Gavor, Edem / Choong, Yeu Khai / Er, Shi Yin / Sivaraman, Hariharan / Sivaraman, J

Trends Immunol

Abstract	The 2019 coronavirus pandemic remains a major public health concern. Neutralizing antibodies (nAbs) represent a cutting-edge antiviral strategy. We focus here on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and SARS-CoV, and discuss current progress in antibody research against rampant SARS-CoV-2 infections. We provide a perspective on the mechanisms of SARS-CoV-2-derived nAbs, comparing these with existing SARS-CoV-derived antibodies. We offer insight into how these antibodies cross-react and cross-neutralize by analyzing available structures of spike (S) glycoprotein-antibody complexes. We also propose ways of adopting antibody-based strategies - such as cocktail antibody therapeutics against SARS-CoV-2 - to overcome the possible resistance of currently identified mutants and mitigate possible antibody-dependent enhancement (ADE) pathologies. This review provides a platform for the progression of antibody and vaccine design against SARS-CoV-2, and possibly against future coronavirus pandemics.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #844007
Database	COVID19

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Article: Structural Basis of SARS-CoV-2- and SARS-CoV-Receptor Binding and Small-Molecule Blockers as Potential Therapeutics

Sivaraman, Hariharan / Er, Shi Yin / Choong, Yeu Khai / Gavor, Edem / Sivaraman, J

Ann. rev. pharmacol. toxicol

Abstract	Over the past two decades, deadly coronaviruses, with the most recent being the severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) 2019 pandemic, have majorly challenged public health. The path for virus invasion into humans and other hosts is mediated by host-pathogen interactions, specifically virus-receptor binding. An in-depth understanding of the virus-receptor binding mechanism is a prerequisite for the discovery of vaccines, antibodies, and small-molecule inhibitors that can interrupt this interaction and prevent or cure infection. In this review, we discuss the viral entry mechanism, the known structural aspects of virus-receptor interactions (SARS-CoV-2 S/humanACE2, SARS-CoV S/humanACE2, and MERS-CoV S/humanDPP4), the key protein domains and amino acid residues involved in binding, and the small-molecule inhibitors and other drugs that have (as of June 2020) exhibited therapeutic potential. Specifically, we review the potential clinical utility of two transmembrane serine protease 2 (TMPRSS2)-targeting protease inhibitors, nafamostat mesylate and camostat mesylate, as well as two novel potent fusion inhibitors and the repurposed Ebola drug, remdesivir, which is specific to RNA-dependent RNA polymerase, against human coronaviruses, including SARS-CoV-2. Expected final online publication date for the Annual Review of Pharmacology and Toxicology, Volume 61 is January 8, 2021. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #612187
Database	COVID19

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