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Article ; Online: Spinal Dysraphism-Histopathological Study of 45 Cases

Bangaru Sandhya / SS Sabitharani / Yandapally Niharikareddy

Journal of Clinical and Diagnostic Research, Vol 15, Iss 6, Pp EC01-EC

2021 Volume 04

Abstract: Introduction: Dysraphic conditions of spine resulting from nonclosure of the neural groove, consists of different types of malformations and they are called spina bifida, which have been classified into several types. Myelomeningocele (MMC) and ... ...

Abstract	Introduction: Dysraphic conditions of spine resulting from nonclosure of the neural groove, consists of different types of malformations and they are called spina bifida, which have been classified into several types. Myelomeningocele (MMC) and Meningocele (MC) come under spina bifida cystica. Aim: Aim of the study was to review the clinical and pathological findings of congenital spinal dysraphism and discuss the pathological diagnosis Materials and Methods: A descriptive cross-sectional type of study was conducted in 45 cases of spinal dysraphism during the period from Oct 2012 to Feb 2016, in the department of pathology of a tertiary care hospital, Hyderabad. Cases which were diagnosed as spinal dysraphism by clinical and radiological examination, tissue specimens were sent to the department of pathology along with clinical and radiological findings. H&E staining was done in all cases, followed by detailed microscopic study of slides. Histopathological findings such as epithelial, mesodermal, neuroectodermal changes were elucidated in detail and findings were compared with literature. Results: In a total of 45 cases there were 30 cases of MMC, nine cases of MC, six cases of encephalocele. Loss of epidermal appendages seen in 91% of cases and neuropil like matrix was present in 76% cases. Conclusion: The embryogenesis of spina bifida involves ectoderm, neuroectoderm and mesoderm. A detailed definition of histopathological aspects will help in understanding these anomalies and should be a part of a detailed histopathology report.
Keywords	encephalocele ; meningocele ; myelomeningocele ; Medicine ; R
Subject code	360
Language	English
Publishing date	2021-06-01T00:00:00Z
Publisher	JCDR Research and Publications Private Limited
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Increasing sensitivity of antibody-antigen interactions using photo-cross-linking.

Torrents de la Peña, Alba / Sewall, Leigh M / de Paiva Froes Rocha, Rebeca / Jackson, Abigail M / Pratap, Payal P / Bangaru, Sandhya / Cottrell, Christopher A / Mohanty, Subhasis / Shaw, Albert C / Ward, Andrew B

Cell reports methods

2023 Volume 3, Issue 6, Page(s) 100509

Abstract: Understanding antibody-antigen interactions in a polyclonal immune response in humans and animal models is critical for rational vaccine design. Current approaches typically characterize antibodies that are functionally relevant or highly abundant. Here, ...

Abstract	Understanding antibody-antigen interactions in a polyclonal immune response in humans and animal models is critical for rational vaccine design. Current approaches typically characterize antibodies that are functionally relevant or highly abundant. Here, we use photo-cross-linking and single-particle electron microscopy to increase antibody detection and unveil epitopes of low-affinity and low-abundance antibodies, leading to a broader structural characterization of polyclonal immune responses. We employed this approach across three different viral glycoproteins and showed increased sensitivity of detection relative to currently used methods. Results were most noticeable in early and late time points of a polyclonal immune response. Additionally, the use of photo-cross-linking revealed intermediate antibody binding states and demonstrated a distinctive way to study antibody binding mechanisms. This technique can be used to structurally characterize the landscape of a polyclonal immune response of patients in vaccination or post-infection studies at early time points, allowing for rapid iterative design of vaccine immunogens.
MeSH term(s)	Animals ; Humans ; Antibodies, Neutralizing ; Epitopes/chemistry ; Vaccination ; Vaccines
Chemical Substances	Antibodies, Neutralizing ; Epitopes ; Vaccines
Language	English
Publishing date	2023-06-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2667-2375
ISSN (online)	2667-2375
DOI	10.1016/j.crmeth.2023.100509
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Histopathological Study of Bone Tumours in 78 Cases from a Tertiary Care Hospital, Hyderabad

Bangaru Sandhya / Thorram Thirupathi / Byrapuram Vijaya Nirmala / Kalla DH PrasannaKumar

National Journal of Laboratory Medicine, Vol 10, Iss 04, Pp 09-

2021 Volume 12

Abstract: Introduction: In comparison with neoplasms in other parts of body, bone tumours are relatively rare. Successful diagnosis and treatment plan of bone tumours involves team approach of pathologist, radiologist, surgeon, oncologist and radiotherapist. As ... ...

Abstract	Introduction: In comparison with neoplasms in other parts of body, bone tumours are relatively rare. Successful diagnosis and treatment plan of bone tumours involves team approach of pathologist, radiologist, surgeon, oncologist and radiotherapist. As histopathology diagnosis is confirmatory in bone tumours, it is very important to make treatment plan and estimation of prognosis in different bone tumours. Current study helps in understanding morphology of different bone tumours, also gives an idea about their age, sex distribution, relative frequencies and location of tumour. Aim: To review the histopathology diagnosis in bone tumours and to evaluate the distribution of different bone tumours according to age, sex and anatomical location, also to evaluate their relative frequencies. Materials and Methods: A cross-sectional study was conducted prospectively in 78 cases for a period of two years from October 2015 to September 2017, in Department of Pathology, Mehdi Nawaz Jung Institute of Oncology, Hyderabad, India and TB and Chest Hospital, Osmania Medical College, Hyderabad. Patients with suspicion of bone tumour on clinical and radiological examination, tissue specimens were referred to Department of Pathology along with essential clinical history such as the age, sex, anatomical site, radiological findings. Haematoxylin and Eosin (H&E) stain was done for all cases, followed by detailed microscopic study of H&E slides. Immunohistochemistry (IHC) marker analysis was performed in selected cases. Histopathology findings were noted. Age, sex, anatomical distribution and relative frequencies of different histological types of bone tumours were evaluated and analysed by comparing with other similar studies. Results: Out of 78 cases of suspected bone tumours, 30 cases were primary malignant bone tumours, 22 were metastatic deposits, 24 were benign tumours, two were chronic osteomyelitis. Osteosarcoma was the most common primary malignant bone tumour and giant cell tumour was most common benign bone tumour. Bone tumours were more common in males than in females most common anatomical location for primary malignant bone tumour was femur followed by tibia secondary deposits were more common in spine followed by pelvis. Conclusion: Histopathology diagnosis is confirmatory in bone tumours. Successful diagnosis of bone tumours is very important to make a treatment plan. Age, sex distribution and anatomical location of different bone tumours correlated well with other previous studies and provided an important role in the definitive diagnosis
Keywords	chondrosarcoma ; ewing’s sarcoma ; giant cell tumour ; osteosarcoma ; Microbiology ; QR1-502 ; Chemistry ; QD1-999
Subject code	616 ; 610
Language	English
Publishing date	2021-10-01T00:00:00Z
Publisher	JCDR Research and Publications Pvt. Ltd.
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Murine Monoclonal Antibodies against the Receptor Binding Domain of SARS-CoV-2 Neutralize Authentic Wild-Type SARS-CoV-2 as Well as B.1.1.7 and B.1.351 Viruses and Protect

Amanat, Fatima / Strohmeier, Shirin / Lee, Wen-Hsin / Bangaru, Sandhya / Ward, Andrew B / Coughlan, Lynda / Krammer, Florian

mBio

2021 Volume 12, Issue 4, Page(s) e0100221

Abstract: After first emerging in late 2019 in China, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has since caused a pandemic leading to millions of infections and deaths worldwide. Vaccines have been developed and authorized, but the supply of ... ...

Abstract	After first emerging in late 2019 in China, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has since caused a pandemic leading to millions of infections and deaths worldwide. Vaccines have been developed and authorized, but the supply of these vaccines is currently limited. With new variants of the virus now emerging and spreading globally, it is essential to develop therapeutics that are broadly protective and bind conserved epitopes in the receptor binding domain (RBD) or the full-length spike protein of SARS-CoV-2. In this study, we generated mouse monoclonal antibodies (MAbs) against different epitopes on the RBD and assessed binding and neutralization of authentic SARS-CoV-2. We demonstrate that antibodies with neutralizing activity, but not nonneutralizing antibodies, lower viral titers in the lungs when administered in a prophylactic setting
MeSH term(s)	Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/immunology ; Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/pharmacology ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; Antibodies, Viral/pharmacology ; Chlorocebus aethiops ; Female ; Humans ; Mice ; Mice, Inbred BALB C ; Neutralization Tests ; Protein Binding ; Protein Domains/immunology ; Receptors, Virus/immunology ; SARS-CoV-2/immunology ; Vero Cells ; Viral Load ; COVID-19 Drug Treatment
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Receptors, Virus ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2021-07-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.01002-21
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Deep repertoire mining uncovers ultra-broad coronavirus neutralizing antibodies targeting multiple spike epitopes.

bioRxiv : the preprint server for biology

2023

Abstract: Development of vaccines and therapeutics that are broadly effective against known and emergent coronaviruses is an urgent priority. Current strategies for developing pan-coronavirus countermeasures have largely focused on the receptor binding domain ( ...

Abstract	Development of vaccines and therapeutics that are broadly effective against known and emergent coronaviruses is an urgent priority. Current strategies for developing pan-coronavirus countermeasures have largely focused on the receptor binding domain (
Language	English
Publishing date	2023-03-31
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.03.28.534602
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Article ; Online: Structural mapping of antibody landscapes to human betacoronavirus spike proteins.

Bangaru, Sandhya / Antanasijevic, Aleksandar / Kose, Nurgun / Sewall, Leigh M / Jackson, Abigail M / Suryadevara, Naveenchandra / Zhan, Xiaoyan / Torres, Jonathan L / Copps, Jeffrey / de la Peña, Alba Torrents / Crowe, James E / Ward, Andrew B

Science advances

2022 Volume 8, Issue 18, Page(s) eabn2911

Abstract: Preexisting immunity against seasonal coronaviruses (CoVs) represents an important variable in predicting antibody responses and disease severity to severe acute respiratory syndrome CoV-2 (SARS-CoV-2) infections. We used electron microscopy-based ... ...

Abstract	Preexisting immunity against seasonal coronaviruses (CoVs) represents an important variable in predicting antibody responses and disease severity to severe acute respiratory syndrome CoV-2 (SARS-CoV-2) infections. We used electron microscopy-based polyclonal epitope mapping (EMPEM) to characterize the antibody specificities against β-CoV spike proteins in prepandemic (PP) sera or SARS-CoV-2 convalescent (SC) sera. We observed that most PP sera had antibodies specific to seasonal human CoVs (HCoVs) OC43 and HKU1 spike proteins while the SC sera showed reactivity across all human β-CoVs. Detailed molecular mapping of spike-antibody complexes revealed epitopes that were differentially targeted by preexisting antibodies and SC serum antibodies. Our studies provide an antigenic landscape to β-HCoV spikes in the general population serving as a basis for cross-reactive epitope analyses in SARS-CoV-2-infected individuals.
MeSH term(s)	Antibodies, Viral ; COVID-19 ; Coronavirus OC43, Human ; Epitopes ; Humans ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus
Chemical Substances	Antibodies, Viral ; Epitopes ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-05-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.abn2911
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Article ; Online: Structure and immune recognition of the porcine epidemic diarrhea virus spike protein.

Kirchdoerfer, Robert N / Bhandari, Mahesh / Martini, Olnita / Sewall, Leigh M / Bangaru, Sandhya / Yoon, Kyoung-Jin / Ward, Andrew B

Structure (London, England : 1993)

2020 Volume 29, Issue 4, Page(s) 385–392.e5

Abstract: Porcine epidemic diarrhea virus (PEDV) is an alphacoronavirus responsible for significant morbidity and mortality in pigs. A key determinant of viral tropism and entry, the PEDV spike protein is a key target for the host antibody response and a good ... ...

Abstract	Porcine epidemic diarrhea virus (PEDV) is an alphacoronavirus responsible for significant morbidity and mortality in pigs. A key determinant of viral tropism and entry, the PEDV spike protein is a key target for the host antibody response and a good candidate for a protein-based vaccine immunogen. We used electron microscopy to evaluate the PEDV spike structure, as well as pig polyclonal antibody responses to viral infection. The structure of the PEDV spike reveals a configuration similar to that of HuCoV-NL63. Several PEDV protein-protein interfaces are mediated by non-protein components, including a glycan at Asn264 and two bound palmitoleic acid molecules. The polyclonal antibody response to PEDV infection shows a dominance of epitopes in the S1 region. This structural and immune characterization provides insights into coronavirus spike stability determinants and explores the immune landscape of viral spike proteins.
MeSH term(s)	Animals ; Antibodies, Viral/metabolism ; Cell Line ; Coronavirus Infections/immunology ; Cryoelectron Microscopy ; Epitopes/immunology ; Fatty Acids, Monounsaturated/chemistry ; Models, Molecular ; Molecular Conformation ; Polysaccharides/chemistry ; Porcine epidemic diarrhea virus/chemistry ; Porcine epidemic diarrhea virus/immunology ; Porcine epidemic diarrhea virus/metabolism ; Protein Binding ; Sf9 Cells ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/immunology ; Swine
Chemical Substances	Antibodies, Viral ; Epitopes ; Fatty Acids, Monounsaturated ; Polysaccharides ; Spike Glycoprotein, Coronavirus ; palmitoleic acid (209B6YPZ4I)
Language	English
Publishing date	2020-12-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2020.12.003
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Article ; Online: Bispecific antibodies combine breadth, potency, and avidity of parental antibodies to neutralize sarbecoviruses.

Radić, Laura / Sliepen, Kwinten / Yin, Victor / Brinkkemper, Mitch / Capella-Pujol, Joan / Schriek, Angela I / Torres, Jonathan L / Bangaru, Sandhya / Burger, Judith A / Poniman, Meliawati / Bontjer, Ilja / Bouhuijs, Joey H / Gideonse, David / Eggink, Dirk / Ward, Andrew B / Heck, Albert J R / Van Gils, Marit J / Sanders, Rogier W / Schinkel, Janke

iScience

2023 Volume 26, Issue 4, Page(s) 106540

Abstract: SARS-CoV-2 variants evade current monoclonal antibody therapies. Bispecific antibodies (bsAbs) combine the specificities of two distinct antibodies taking advantage of the avidity and synergy provided by targeting different epitopes. Here we used ... ...

Abstract	SARS-CoV-2 variants evade current monoclonal antibody therapies. Bispecific antibodies (bsAbs) combine the specificities of two distinct antibodies taking advantage of the avidity and synergy provided by targeting different epitopes. Here we used controlled Fab-arm exchange to produce bsAbs that neutralize SARS-CoV and SARS-CoV-2 variants, including Omicron and its subvariants, by combining potent SARS-CoV-2-specific neutralizing antibodies with broader antibodies that also neutralize SARS-CoV. We demonstrated that the parental antibodies rely on avidity for neutralization using bsAbs containing one irrelevant Fab arm. Using mass photometry to measure the formation of antibody:spike complexes, we determined that bsAbs increase binding stoichiometry compared to corresponding cocktails, without a loss of binding affinity. The heterogeneous binding pattern of bsAbs to spike, observed by negative-stain electron microscopy and mass photometry provided evidence for both intra- and inter-spike crosslinking. This study highlights the utility of cross-neutralizing antibodies for designing bivalent agents to combat circulating and future SARS-like coronaviruses.
Language	English
Publishing date	2023-03-31
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2023.106540
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Article ; Online: Structure and immune recognition of the porcine epidemic diarrhea virus spike protein

Kirchdoerfer, Robert N. / Bhandari, Mahesh / Martini, Olnita / Sewall, Leigh M. / Bangaru, Sandhya / Yoon, Kyoung-Jin / Ward, Andrew B.

bioRxiv

Keywords	covid19
Language	English
Publishing date	2020-02-19
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.02.18.955195
Database	COVID19

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Article ; Online: Human antibody recognition of H7N9 influenza virus HA following natural infection.

Gilchuk, Iuliia M / Bangaru, Sandhya / Kose, Nurgun / Bombardi, Robin G / Trivette, Andrew / Li, Sheng / Turner, Hannah L / Carnahan, Robert H / Ward, Andrew B / Crowe, James E

JCI insight

2021 Volume 6, Issue 19

Abstract: Avian H7N9 influenza viruses cause sporadic outbreaks of human infections and threaten to cause a major pandemic. The breadth of B cell responses to natural infection and the dominant antigenic sites recognized during first exposure to H7 HA following ... ...

Abstract	Avian H7N9 influenza viruses cause sporadic outbreaks of human infections and threaten to cause a major pandemic. The breadth of B cell responses to natural infection and the dominant antigenic sites recognized during first exposure to H7 HA following infection are incompletely understood. Here, we studied the B cell response to H7 HA of 2 individuals who had recovered from natural H7N9 virus infection. We used competition binding, hydrogen-deuterium mass spectrometry, and single-particle negative stain electron microscopy to identify the patterns of molecular recognition of the antibody responses to H7 HA. We found that circulating H7-reactive B cells recognized a diverse antigenic landscape on the HA molecule, including HA head domain epitopes in antigenic sites A and B and in the trimer interface-II region and epitopes in the stem region. Most H7 antibodies exhibited little heterosubtypic breadth, but many recognized a wide diversity of unrelated H7 strains. We tested the antibodies for functional activity and identified clones with diverse patterns of inhibition, including neutralizing, hemagglutination- or egress-inhibiting, or HA trimer-disrupting activities. Thus, the human B cell response to primary H7 natural infection is diverse, highly functional, and broad for recognition of diverse H7 strains.
MeSH term(s)	Antibodies, Viral/immunology ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Humans ; Influenza A Virus, H7N9 Subtype/immunology ; Influenza, Human/immunology
Chemical Substances	Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus ; hemagglutinin, avian influenza A virus
Language	English
Publishing date	2021-10-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.152403
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