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1. 原発性免疫不全症の診断のためのフローサイトメトリー flow cytometry for the diagnosis of primary immunodeficiencies
2. 血球貪食リンパ組織球の臨床的特徴および診断 clinical features and diagnosis of hemophagocytic lymphohistiocytosis

English Journal

Family-based analysis identified CD2 as a susceptibility gene for primary open angle glaucoma in Chinese Han population.

Liu T1, Xie L, Ye J, He X.Author information 1Department of Ophthalmology, Daping Hospital & Research Institute of Surgery, Third Military Medical University of PLA, Chongqing, China.AbstractPrimary open angle glaucoma (POAG) is characterized by optic disc cupping and irreversible loss of retinal ganglion cells. Few genes have been detected that influence POAG susceptibility and little is known about its genetic architecture. In this study, we employed exome sequencing on three members from a high frequency POAG family to identify the risk factors of POAG in Chinese population. Text-mining method was applied to identify genes associated with glaucoma in literature, and protein-protein interaction networks were constructed. Furthermore, reverse transcription PCR and Western blot were performed to confirm the differential gene expression. Six genes, baculoviral inhibitors of apoptosis protein repeat containing 6 (BIRC6), CD2, luteinizing hormone/choriogonadotropin receptor (LHCGR), polycystic kidney and hepatic disease gene 1 (PKHD1), phenylalanine hydroxylase (PAH) and fucosyltransferase 7 (FUT7), which might be associated with POAG, were identified. Both the mRNA expression levels and protein expression levels of HSP27 were increased in astrocytes from POAG patients compared with those from normal control, suggesting that mutation in CD2 might pose a risk for POAG in Chinese population. In conclusion, novel rare variants detected by exome sequencing may hold the key to unravelling the remaining contribution of genetics to complex diseases such as POAG.
Journal of cellular and molecular medicine.J Cell Mol Med.2014 Apr;18(4):600-9. doi: 10.1111/jcmm.12201. Epub 2014 Mar 6.
Primary open angle glaucoma (POAG) is characterized by optic disc cupping and irreversible loss of retinal ganglion cells. Few genes have been detected that influence POAG susceptibility and little is known about its genetic architecture. In this study, we employed exome sequencing on three members
PMID 24597656

Analysis of a chitinase from EpapGV, a fast killing betabaculovirus.

Salvador R1, Ferrelli ML, Sciocco-Cap A, Romanowski V.Author information 1Instituto de Microbiología y Zoología Agrícola, IMYZA-CICVyA-INTA, CC 25 (B1712WAA), Castelar, Buenos Aires, Argentina, rsalvador@cnia.inta.gov.ar.AbstractThe main function of baculoviral chitinase protein (V-CHIA) is to promote the final liquefaction of infected host larvae, facilitating the dispersion of occlusion bodies (OBs) in the environment. In this study, a v-chiA from Epinotia aporema Granulovirus (EpapGV) was identified and characterized. The 1,713 base pairs long open reading frame encodes a protein of 570 amino acids with a predicted molecular weight of 63 kDa. EpapGV V-CHIA sequence alignment resulted 62 % identical to Pieris rapae GV and Blastp search revealed a high conservation among all baculovirus chitinases. Amino acid sequence analysis indicated that the C-terminal KDEL present in most alphabaculovirus chitinases is absent in EpapGV V-CHIA, as well as in the rest of the betabaculoviruses. Phylogenetic analysis was performed with bacterial, lepidopteran, and baculoviral chitinase sequences available in databases. Using an AcMNPV bacmid (bApGOZA) a recombinant Ac-chiAEpapGV was obtained in order to overexpress EpapGV V-CHIA in cell culture. The presence of chitinase was detected in purified AcMNPV-chiAEpapGV OBs. Peritrophic membranes of Anticarsia gemmatalis larvae fed with recombinant OBs showed an altered structure. The results presented in this study show that EpapGV chitinase overexpression in recombinant baculovirus can cause association of this protein with OBs, and suggest that this could be used to evaluate the protein role in early stages of baculoviral infections.
Virus genes.Virus Genes.2014 Apr;48(2):406-9. doi: 10.1007/s11262-013-1019-7. Epub 2013 Dec 3.
The main function of baculoviral chitinase protein (V-CHIA) is to promote the final liquefaction of infected host larvae, facilitating the dispersion of occlusion bodies (OBs) in the environment. In this study, a v-chiA from Epinotia aporema Granulovirus (EpapGV) was identified and characterized. Th
PMID 24297310

Expression and nuclear localization of the TATA-binding protein during baculovirus infection.

Mainz D1, Quadt I, Stranzenbach AK, Voss D, Guarino LA, Knebel-Moersdorf D.Author information 1Center for Biochemistry, University of Cologne, Germany;AbstractThe TATA box binding protein (TBP) plays a key role in initiating eukaryotic transcription and is used by many viruses for viral transcription. We previously reported increased TBP levels during the infection with the baculovirus Autographa californica multicapsid nuclear polyhedrovirus (AcMNPV). The TBP antiserum used in that study, however, cross-reacted with a baculoviral protein. Here, we report that with a TBP-specific antiserum increased amounts of nuclear TBP were detected upon infection of S. frugipeda and TN-368 cells. TBP levels increased until 72 h p.i. while tbp transcripts decreased by 16 h p.i. which suggests a virus-induced influence on the TBP protein levels. To address a potential modification of the TBP degradation pathway during infection, we investigated the possible role of viral ubiquitin. Infection studies with AcMNPV recombinants carrying a mutated viral ubiquitin gene revealed that the TBP increase during infection was not altered. In addition, pulse-chase experiments indicated a high TBP half-life of about 60 h in uninfected cells, suggesting that a virus-induced increase of TBP stability was unlikely. This increase in TBP correlated with a redistribution to nuclear domains resembling sites of viral DNA synthesis. Furthermore, we observed colocalization of TBP with host RNA polymerase II (RNAPII), but only until 8 h p.i. while TBP, but not RNAPII, was present in the enlarged replication domains late during infection. Thus, we suggest that AcMNPV adapted a mechanism to accumulate the higly stable cellular TBP at sites of viral DNA replication and transcription.
The Journal of general virology.J Gen Virol.2014 Mar 27. doi: 10.1099/vir.0.059949-0. [Epub ahead of print]
The TATA box binding protein (TBP) plays a key role in initiating eukaryotic transcription and is used by many viruses for viral transcription. We previously reported increased TBP levels during the infection with the baculovirus Autographa californica multicapsid nuclear polyhedrovirus (AcMNPV). Th
PMID 24676420

Japanese Journal

Baculoviral IAP2 and IAP3 encoded by Lymantria xylina multiple nucleopolyhedrovirus (LyxyMNPV) suppress insect cell apoptosis in a transient expression assay