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Article: The Underrated Gut Microbiota Helminths, Bacteriophages, Fungi, and Archaea.

Garcia-Bonete, Maria Jose / Rajan, Anandi / Suriano, Francesco / Layunta, Elena

2023 Volume 13, Issue 8

Abstract: The microbiota inhabits the gastrointestinal tract, providing essential capacities to the host. The microbiota is a crucial factor in intestinal health and regulates intestinal physiology. However, microbiota disturbances, named dysbiosis, can disrupt ... ...

Abstract	The microbiota inhabits the gastrointestinal tract, providing essential capacities to the host. The microbiota is a crucial factor in intestinal health and regulates intestinal physiology. However, microbiota disturbances, named dysbiosis, can disrupt intestinal homeostasis, leading to the development of diseases. Classically, the microbiota has been referred to as bacteria, though other organisms form this complex group, including viruses, archaea, and eukaryotes such as fungi and protozoa. This review aims to clarify the role of helminths, bacteriophages, fungi, and archaea in intestinal homeostasis and diseases, their interaction with bacteria, and their use as therapeutic targets in intestinal maladies.
Language	English
Publishing date	2023-08-18
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2662250-6
ISSN	2075-1729
ISSN	2075-1729
DOI	10.3390/life13081765
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Article ; Online: Heparan Sulfate Is a Cellular Receptor for Enteric Human Adenoviruses.

Rajan, Anandi / Palm, Elin / Trulsson, Fredrik / Mundigl, Sarah / Becker, Miriam / Persson, B David / Frängsmyr, Lars / Lenman, Annasara

Viruses

2021 Volume 13, Issue 2

Abstract: Human adenovirus (HAdV)-F40 and -F41 are leading causes of diarrhea and diarrhea-associated mortality in children under the age of five, but the mechanisms by which they infect host cells are poorly understood. HAdVs initiate infection through ... ...

Abstract	Human adenovirus (HAdV)-F40 and -F41 are leading causes of diarrhea and diarrhea-associated mortality in children under the age of five, but the mechanisms by which they infect host cells are poorly understood. HAdVs initiate infection through interactions between the knob domain of the fiber capsid protein and host cell receptors. Unlike most other HAdVs, HAdV-F40 and -F41 possess two different fiber proteins-a long fiber and a short fiber. Whereas the long fiber binds to the Coxsackievirus and adenovirus receptor (CAR), no binding partners have been identified for the short fiber. In this study, we identified heparan sulfate (HS) as an interaction partner for the short fiber of enteric HAdVs. We demonstrate that exposure to acidic pH, which mimics the environment of the stomach, inactivates the interaction of enteric adenovirus with CAR. However, the short fiber:HS interaction is resistant to and even enhanced by acidic pH, which allows attachment to host cells. Our results suggest a switch in receptor usage of enteric HAdVs after exposure to acidic pH and add to the understanding of the function of the short fibers. These results may also be useful for antiviral drug development and the utilization of enteric HAdVs for clinical applications such as vaccine development.
MeSH term(s)	Adenovirus Infections, Human/metabolism ; Adenovirus Infections, Human/virology ; Adenoviruses, Human/chemistry ; Adenoviruses, Human/genetics ; Adenoviruses, Human/metabolism ; Capsid Proteins/chemistry ; Capsid Proteins/genetics ; Capsid Proteins/metabolism ; Child, Preschool ; Female ; Heparitin Sulfate/metabolism ; Humans ; Infant ; Male ; Protein Domains ; Receptors, Virus/metabolism
Chemical Substances	Capsid Proteins ; Receptors, Virus ; adenovirus receptor ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2021-02-14
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13020298
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Article ; Online: Heparan Sulfate Is a Cellular Receptor for Enteric Human Adenoviruses.

Rajan, Anandi / Palm, Elin / Trulsson, Fredrik / Mundigl, Sarah / Becker, Miriam / Persson, B David / Frängsmyr, Lars / Lenman, Annasara

13 ; 2 ; Viruses ; Switzerland

2021

Abstract	Human adenovirus (HAdV)-F40 and -F41 are leading causes of diarrhea and diarrhea-associated mortality in children under the age of five, but the mechanisms by which they infect host cells are poorly understood. HAdVs initiate infection through interactions between the knob domain of the fiber capsid protein and host cell receptors. Unlike most other HAdVs, HAdV-F40 and -F41 possess two different fiber proteins-a long fiber and a short fiber. Whereas the long fiber binds to the Coxsackievirus and adenovirus receptor (CAR), no binding partners have been identified for the short fiber. In this study, we identified heparan sulfate (HS) as an interaction partner for the short fiber of enteric HAdVs. We demonstrate that exposure to acidic pH, which mimics the environment of the stomach, inactivates the interaction of enteric adenovirus with CAR. However, the short fiber:HS interaction is resistant to and even enhanced by acidic pH, which allows attachment to host cells. Our results suggest a switch in receptor usage of enteric HAdVs after exposure to acidic pH and add to the understanding of the function of the short fibers. These results may also be useful for antiviral drug development and the utilization of enteric HAdVs for clinical applications such as vaccine development.
Keywords	capsid proteins ; enteric adenovirus ; fiber knobs ; heparan sulfate ; short fibers
Subject code	572
Language	English
Publishing date	2021-02-14
Publisher	MDPI
Publishing country	de
Document type	Article ; Online
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Article ; Online: Interaction of Human Enterochromaffin Cells with Human Enteric Adenovirus 41 Leads to Serotonin Release and Subsequent Activation of Enteric Glia Cells.

Westerberg, Sonja / Hagbom, Marie / Rajan, Anandi / Loitto, Vesa / Persson, B David / Allard, Annika / Nordgren, Johan / Sharma, Sumit / Magnusson, Karl-Eric / Arnberg, Niklas / Svensson, Lennart

Journal of virology

2018 Volume 92, Issue 7

Abstract: Human adenovirus 41 (HAdV-41) causes acute gastroenteritis in young children. The main characteristics of HAdV-41 infection are diarrhea and vomiting. Nevertheless, the precise mechanism of HAdV-41-induced diarrhea is unknown, as a suitable small-animal ... ...

Abstract	Human adenovirus 41 (HAdV-41) causes acute gastroenteritis in young children. The main characteristics of HAdV-41 infection are diarrhea and vomiting. Nevertheless, the precise mechanism of HAdV-41-induced diarrhea is unknown, as a suitable small-animal model has not been described. In this study, we used the human midgut carcinoid cell line GOT1 to investigate the effect of HAdV-41 infection and the individual HAdV-41 capsid proteins on serotonin release by enterochromaffin cells and on enteric glia cell (EGC) activation. We first determined that HAdV-41 could infect the enterochromaffin cells. Immunofluorescence staining revealed that the cells expressed HAdV-41-specific coxsackievirus and adenovirus receptor (CAR); flow cytometry analysis supported these findings. HAdV-41 infection of the enterochromaffin cells induced serotonin secretion dose dependently. In contrast, control infection with HAdV-5 did not induce serotonin secretion in the cells. Confocal microscopy studies of enterochromaffin cells infected with HAdV-41 revealed decreased serotonin immunofluorescence compared to that in uninfected cells. Incubation of the enterochromaffin cells with purified HAdV-41 short fiber knob and hexon proteins increased the serotonin levels in the harvested cell supernatant significantly. HAdV-41 infection could also activate EGCs, as shown in the significantly altered expression of glia fibrillary acidic protein (GFAP) in EGCs incubated with HAdV-41. The EGCs were also activated by serotonin alone, as shown in the significantly increased GFAP staining intensity. Likewise, EGCs were activated by the cell supernatant of HAdV-41-infected enterochromaffin cells.
MeSH term(s)	A549 Cells ; Adenoviridae/metabolism ; Adenoviridae Infections/metabolism ; Adenoviridae Infections/pathology ; Coxsackie and Adenovirus Receptor-Like Membrane Protein/metabolism ; Enterochromaffin Cells/metabolism ; Enterochromaffin Cells/pathology ; Enterochromaffin Cells/virology ; Glial Fibrillary Acidic Protein/metabolism ; Humans ; Neuroglia/pathology ; Neuroglia/secretion ; Neuroglia/virology ; Serotonin/secretion
Chemical Substances	Coxsackie and Adenovirus Receptor-Like Membrane Protein ; Glial Fibrillary Acidic Protein ; Serotonin (333DO1RDJY)
Language	English
Publishing date	2018-03-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00026-18
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Article ; Online: Enteric Species F Human Adenoviruses use Laminin-Binding Integrins as Co-Receptors for Infection of Ht-29 Cells.

Rajan, Anandi / Persson, B David / Frängsmyr, Lars / Olofsson, Annelie / Sandblad, Linda / Heino, Jyrki / Takada, Yoshikazu / Mould, A Paul / Schnapp, Lynn M / Gall, Jason / Arnberg, Niklas

Scientific reports

2018 Volume 8, Issue 1, Page(s) 10019

Abstract: The enteric species F human adenovirus types 40 and 41 (HAdV-40 and -41) are the third most common cause of infantile gastroenteritis in the world. Knowledge about HAdV-40 and -41 cellular infection is assumed to be fundamentally different from that of ... ...

Abstract	The enteric species F human adenovirus types 40 and 41 (HAdV-40 and -41) are the third most common cause of infantile gastroenteritis in the world. Knowledge about HAdV-40 and -41 cellular infection is assumed to be fundamentally different from that of other HAdVs since HAdV-40 and -41 penton bases lack the αV-integrin-interacting RGD motif. This motif is used by other HAdVs mainly for internalization and endosomal escape. We hypothesised that the penton bases of HAdV-40 and -41 interact with integrins independently of the RGD motif. HAdV-41 transduction of a library of rodent cells expressing specific human integrin subunits pointed to the use of laminin-binding α2-, α3- and α6-containing integrins as well as other integrins as candidate co-receptors. Specific laminins prevented internalisation and infection, and recombinant, soluble HAdV-41 penton base proteins prevented infection of human intestinal HT-29 cells. Surface plasmon resonance analysis demonstrated that HAdV-40 and -41 penton base proteins bind to α6-containing integrins with an affinity similar to that of previously characterised penton base:integrin interactions. With these results, we propose that laminin-binding integrins are co-receptors for HAdV-40 and -41.
MeSH term(s)	Adenoviruses, Human/metabolism ; Animals ; CHO Cells ; Cell Line ; Cricetulus ; HT29 Cells ; Humans ; Integrin alpha6/metabolism ; Integrin alpha6beta4/metabolism ; Laminin/metabolism ; Receptors, Virus/metabolism ; Surface Plasmon Resonance ; Virus Attachment
Chemical Substances	Integrin alpha6 ; Integrin alpha6beta4 ; Laminin ; Receptors, Virus
Language	English
Publishing date	2018-07-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-28255-7
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Article ; Online: Adenovirus-based vaccines for fighting infectious diseases and cancer: progress in the field.

Majhen, Dragomira / Calderon, Hugo / Chandra, Naresh / Fajardo, Carlos Alberto / Rajan, Anandi / Alemany, Ramon / Custers, Jerome

Human gene therapy

2014 Volume 25, Issue 4, Page(s) 301–317

Abstract: The field of adenovirology is undergoing rapid change in response to increasing appreciation of the potential advantages of adenoviruses as the basis for new vaccines and as vectors for gene and cancer therapy. Substantial knowledge and understanding of ... ...

Abstract	The field of adenovirology is undergoing rapid change in response to increasing appreciation of the potential advantages of adenoviruses as the basis for new vaccines and as vectors for gene and cancer therapy. Substantial knowledge and understanding of adenoviruses at a molecular level has made their manipulation for use as vaccines and therapeutics relatively straightforward in comparison with other viral vectors. In this review we summarize the structure and life cycle of the adenovirus and focus on the use of adenovirus-based vectors in vaccines against infectious diseases and cancers. Strategies to overcome the problem of preexisting antiadenovirus immunity, which can hamper the immunogenicity of adenovirus-based vaccines, are discussed. When armed with tumor-associated antigens, replication-deficient and oncolytic adenoviruses can efficiently activate an antitumor immune response. We present concepts on how to use adenoviruses as therapeutic cancer vaccines and consider some of the strategies used to further improve antitumor immune responses. Studies that explore the prospect of adenoviruses as vaccines against infectious diseases and cancer are underway, and here we give an overview of the latest developments.
MeSH term(s)	Adaptive Immunity ; Adenoviridae/immunology ; Adenoviridae/physiology ; Animals ; Cancer Vaccines ; Communicable Disease Control ; Communicable Diseases/immunology ; Genetic Therapy ; Genetic Vectors/genetics ; Genetic Vectors/immunology ; Humans ; Immunity, Innate ; Neoplasms/immunology ; Neoplasms/therapy ; Vaccines, Synthetic/genetics ; Vaccines, Synthetic/immunology
Chemical Substances	Cancer Vaccines ; Vaccines, Synthetic
Language	English
Publishing date	2014-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1028152-6
ISSN	1557-7422 ; 1043-0342
ISSN (online)	1557-7422
ISSN	1043-0342
DOI	10.1089/hum.2013.235
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Article ; Online: Human adenovirus 52 uses sialic acid-containing glycoproteins and the coxsackie and adenovirus receptor for binding to target cells.

Lenman, Annasara / Liaci, A Manuel / Liu, Yan / Årdahl, Carin / Rajan, Anandi / Nilsson, Emma / Bradford, Will / Kaeshammer, Lisa / Jones, Morris S / Frängsmyr, Lars / Feizi, Ten / Stehle, Thilo / Arnberg, Niklas

PLoS pathogens

2015 Volume 11, Issue 2, Page(s) e1004657

Abstract: Most adenoviruses attach to host cells by means of the protruding fiber protein that binds to host cells via the coxsackievirus and adenovirus receptor (CAR) protein. Human adenovirus type 52 (HAdV-52) is one of only three gastroenteritis-causing HAdVs ... ...

Abstract	Most adenoviruses attach to host cells by means of the protruding fiber protein that binds to host cells via the coxsackievirus and adenovirus receptor (CAR) protein. Human adenovirus type 52 (HAdV-52) is one of only three gastroenteritis-causing HAdVs that are equipped with two different fiber proteins, one long and one short. Here we show, by means of virion-cell binding and infection experiments, that HAdV-52 can also attach to host cells via CAR, but most of the binding depends on sialylated glycoproteins. Glycan microarray, flow cytometry, surface plasmon resonance and ELISA analyses reveal that the terminal knob domain of the long fiber (52LFK) binds to CAR, and the knob domain of the short fiber (52SFK) binds to sialylated glycoproteins. X-ray crystallographic analysis of 52SFK in complex with 2-O-methylated sialic acid combined with functional studies of knob mutants revealed a new sialic acid binding site compared to other, known adenovirus:glycan interactions. Our findings shed light on adenovirus biology and may help to improve targeting of adenovirus-based vectors for gene therapy.
MeSH term(s)	Adenoviruses, Human/chemistry ; Adenoviruses, Human/physiology ; Base Sequence ; Cell Line ; Coxsackie and Adenovirus Receptor-Like Membrane Protein/chemistry ; Coxsackie and Adenovirus Receptor-Like Membrane Protein/metabolism ; Crystallography, X-Ray ; Glycoproteins/chemistry ; Glycoproteins/metabolism ; Humans ; Molecular Sequence Data ; Viral Proteins/chemistry ; Viral Proteins/metabolism ; Viral Tropism/physiology ; Virus Attachment
Chemical Substances	Coxsackie and Adenovirus Receptor-Like Membrane Protein ; Glycoproteins ; Viral Proteins
Language	English
Publishing date	2015-02-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1004657
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Article ; Online: 14-3-3γ-Mediated transport of plakoglobin to the cell border is required for the initiation of desmosome assembly in vitro and in vivo.

Journal of cell science

2014 Volume 127, Issue Pt 10, Page(s) 2174–2188

Abstract: The regulation of cell-cell adhesion is important for the processes of tissue formation and morphogenesis. Here, we report that loss of 14-3-3γ leads to a decrease in cell-cell adhesion and a defect in the transport of plakoglobin and other desmosomal ... ...

Abstract	The regulation of cell-cell adhesion is important for the processes of tissue formation and morphogenesis. Here, we report that loss of 14-3-3γ leads to a decrease in cell-cell adhesion and a defect in the transport of plakoglobin and other desmosomal proteins to the cell border in HCT116 cells and cells of the mouse testis. 14-3-3γ binds to plakoglobin in a PKCμ-dependent fashion, resulting in microtubule-dependent transport of plakoglobin to cell borders. Transport of plakoglobin to the border is dependent on the KIF5B-KLC1 complex. Knockdown of KIF5B in HCT116 cells, or in the mouse testis, results in a phenotype similar to that observed upon 14-3-3γ knockdown. Our results suggest that loss of 14-3-3γ leads to decreased desmosome formation and a decrease in cell-cell adhesion in vitro, and in the mouse testis in vivo, leading to defects in testis organization and spermatogenesis.
MeSH term(s)	14-3-3 Proteins/metabolism ; Animals ; Biological Transport ; Cell Adhesion/physiology ; Desmosomes/metabolism ; HCT116 Cells ; Humans ; In Vitro Techniques ; Infertility, Male/metabolism ; Male ; Mice ; gamma Catenin/metabolism
Chemical Substances	14-3-3 Proteins ; gamma Catenin
Language	English
Publishing date	2014-05-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.125807
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Article: The Underrated Gut Microbiota Helminths, Bacteriophages, Fungi, and Archaea.

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Article ; Online: Heparan Sulfate Is a Cellular Receptor for Enteric Human Adenoviruses.

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Article ; Online: Heparan Sulfate Is a Cellular Receptor for Enteric Human Adenoviruses.

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Article ; Online: Interaction of Human Enterochromaffin Cells with Human Enteric Adenovirus 41 Leads to Serotonin Release and Subsequent Activation of Enteric Glia Cells.

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Article ; Online: Enteric Species F Human Adenoviruses use Laminin-Binding Integrins as Co-Receptors for Infection of Ht-29 Cells.

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Article ; Online: Adenovirus-based vaccines for fighting infectious diseases and cancer: progress in the field.

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Article ; Online: Human adenovirus 52 uses sialic acid-containing glycoproteins and the coxsackie and adenovirus receptor for binding to target cells.

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Article ; Online: 14-3-3γ-Mediated transport of plakoglobin to the cell border is required for the initiation of desmosome assembly in vitro and in vivo.

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