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5. The habitat disruption induces immune-suppression and oxidative stress in honey bees

Author

Morimoto, Tomomi, Kojima, Yuriko, Toki, Taku, Komeda, Yayoi, Yoshiyama, Mikio, Kimura, Kiyoshi, Nirasawa, Keijiro, and Kadowaki, Tatsuhiko

Subjects
pollination, Greenhouse, honey bee, immune-suppression, oxidative stress, habitat degradation, Original Research
Abstract

The honey bee is a major insect used for pollination of many commercial crops worldwide. Although the use of honey bees for pollination can disrupt the habitat, the effects on their physiology have never been determined. Recently, honey bee colonies have often collapsed when introduced in greenhouses for pollination in Japan. Thus, suppressing colony collapses and maintaining the number of worker bees in the colonies is essential for successful long-term pollination in greenhouses and recycling of honey bee colonies. To understand the physiological states of honey bees used for long-term pollination in greenhouses, we characterized their gene expression profiles by microarray. We found that the greenhouse environment changes the gene expression profiles and induces immune-suppression and oxidative stress in honey bees. In fact, the increase of the number of Nosema microsporidia and protein carbonyl content was observed in honey bees during pollination in greenhouses. Thus, honey bee colonies are likely to collapse during pollination in greenhouses when heavily infested with pathogens. Degradation of honey bee habitat by changing the outside environment of the colony, during pollination services for example, imposes negative impacts on honey bees. Thus, worldwide use of honey bees for crop pollination in general could be one of reasons for the decline of managed honey bee colonies.

Published
2011

11. A single-amino-acid substitution in herpes simplex virus 1 envelope glycoprotein B at a site required for binding to the paired immunoglobulin-like type 2 receptor alpha (PILRalpha) abrogates PILRalpha-dependent viral entry and reduces pathogenesis.

Author

Arii J, Wang J, Morimoto T, Suenaga T, Akashi H, Arase H, and Kawaguchi Y

Subjects
Amino Acid Substitution, Animals, Base Sequence, Binding Sites genetics, Cell Line, DNA Primers genetics, Female, Glycosylation, Herpesvirus 1, Human physiology, Host-Pathogen Interactions genetics, Host-Pathogen Interactions physiology, Humans, Membrane Fusion genetics, Membrane Fusion physiology, Mice, Mice, Inbred ICR, Mutant Proteins genetics, Mutant Proteins physiology, Recombinant Proteins genetics, Recombinant Proteins metabolism, Viral Envelope Proteins physiology, Virulence genetics, Virulence physiology, Virus Internalization, Virus Replication genetics, Virus Replication physiology, Herpesvirus 1, Human genetics, Herpesvirus 1, Human pathogenicity, Receptors, Immunologic physiology, Viral Envelope Proteins genetics
Abstract

Paired immunoglobulin-like type 2 receptor α (PILRα) is a herpes simplex virus 1 (HSV-1) entry receptor that associates with O-glycans on HSV-1 envelope glycoprotein B (gB). Two threonine residues (Thr-53 and Thr-480) in gB, which are required for the addition of the principal gB O-glycans, are essential for binding to soluble PILRα. However, the role of the two threonines in PILRα-dependent viral entry remains to be elucidated. Therefore, we constructed a recombinant HSV-1 carrying an alanine replacement of gB Thr-53 alone (gB-T53A) or of both gB Thr-53 and Thr-480 (gB-T53/480A) and demonstrated that these mutations abrogated viral entry in CHO cells expressing PILRα. In contrast, the mutations had no effect on viral entry in CHO cells expressing known host cell receptors for HSV-1 gD, viral entry in HL60 cells expressing myelin-associated glycoprotein (MAG) (another HSV-1 gB receptor), viral attachment to heparan sulfate, and viral replication in PILRα-negative cells. These results support the hypothesis that gB Thr-53 and Thr-480 as well as gB O-glycosylation, probably at these sites, are critical for PILRα-dependent viral entry. Interestingly, following corneal inoculation in mice, the gB-T53A and gB-T53/480A mutations significantly reduced viral replication in the cornea, the development of herpes stroma keratitis, and neuroinvasiveness. The abilities of HSV-1 to enter cells in a PILRα-dependent manner and to acquire specific carbohydrates on gB are therefore linked to an increase in viral replication and virulence in the experimental murine model.

Published
2010
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12. Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor alpha.

Author

Arii J, Uema M, Morimoto T, Sagara H, Akashi H, Ono E, Arase H, and Kawaguchi Y

Subjects
Adenosine Triphosphate biosynthesis, Alphaherpesvirinae genetics, Alphaherpesvirinae ultrastructure, Animals, Cells, Cultured, Chlorocebus aethiops, Cricetinae, Endocytosis, Leukocytes, Mononuclear immunology, Lipopolysaccharide Receptors immunology, Membrane Glycoproteins genetics, Microscopy, Electron, Protein Binding, Receptors, Immunologic genetics, Transgenes, Alphaherpesvirinae metabolism, Membrane Glycoproteins metabolism, Receptors, Immunologic metabolism, Virus Internalization
Abstract

Herpes simplex virus 1 (HSV-1) enters cells either via fusion of the virion envelope and host cell plasma membrane or via endocytosis, depending on the cell type. In the study reported here, we investigated a viral entry pathway dependent on the paired immunoglobulin-like type 2 receptor alpha (PILRalpha), a recently identified entry coreceptor for HSV-1 that associates with viral envelope glycoprotein B (gB). Experiments using inhibitors of endocytic pathways and ultrastructural analyses of Chinese hamster ovary (CHO) cells transduced with PILRalpha showed that HSV-1 entry into these cells was via virus-cell fusion at the cell surface. Together with earlier observations that HSV-1 uptake into normal CHO cells and those transduced with a receptor for HSV-1 envelope gD is mediated by endocytosis, these results indicated that expression of PILRalpha produced an alternative HSV-1 entry pathway in CHO cells. We also showed that human and murine PILRalpha were able to mediate entry of pseudorabies virus, a porcine alphaherpesvirus, but not of HSV-2. These results indicated that viral entry via PILRalpha appears to be conserved but that there is a PILRalpha preference among alphaherpesviruses.

Published
2009
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