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K M Haan

Publications and source records attributed to K M Haan.

5 recordsLinked to original sources
PubMed2001

Different functional domains in the cytoplasmic tail of glycoprotein B are involved in Epstein-Barr virus-induced membrane fusion.

A virus-free cell fusion assay relying on the transient transfection of Epstein-Barr virus (EBV) glycoproteins into cells provides an efficient and quantitative assay for characterizing the viral requirements necessary for fusion of the viral envelope with the B cell membrane. Extensive cellular fusion occurred when Daudi cells were layered onto Chinese hamster ovary K1 cells transiently expressing EBV glycoproteins gp42, gH, gL, and gB. This is the first direct evidence that gB is involved in the process of EBV entry. Moreover, mutational analysis of gB indicates that the cytoplasmic tail contains two distinct domains that function differentially in the process of fusion. The region from amino acids 802 to 816 is necessary for productive membrane fusion, while amino acids 817 to 841 comprise a domain that negatively regulates membrane fusion.

Amino Acid Sequence↗
PubMed2001

Establishment of latent Epstein-Barr virus infection and stable episomal maintenance in murine B-cell lines.

Epstein-Barr virus (EBV) is a strict human pathogen for which no small animal models exist. Plasmids that contain the EBV plasmid origin of replication, oriP, and express EBV nuclear antigen 1 (EBNA1) are stably maintained extrachromosomally in human cells, whereas these plasmids replicate poorly in rodent cells. However, the ability of oriP and EBNA1 to maintain the entire EBV episome in proliferating rodent cells has not been determined. Expression of the two human B-cell receptors for EBV on the surfaces of murine B cells allows efficient viral entry that leads to the establishment of latent EBV infection and long-term persistence of the viral genome. Latent gene expression in these cells resembles the latency II profile in that EBNA1 and LMP1 can be detected whereas EBNA2 and the EBNA3s are not expressed.

Animals↗
PubMed2000

Coreceptor restriction within the HLA-DQ locus for Epstein-Barr virus infection.

Epstein-Barr virus (EBV) is a ubiquitous human herpesvirus that causes infectious mononucleosis and is etiologically associated with malignancies of multiple origins. EBV enters cells through a cascade of interactions between its envelope glycoprotein gp350 and the gp42-gH-gL complex with cellular receptors. Membrane fusion is catalyzed by the binding of gp42, a member of the C type lectin family, to HLA class II molecule HLA-DR, -DP, or -DQ. Here we demonstrate that only a subset of HLA-DQ alleles mediates EBV entry, indicating that individuals expressing these alleles may offer unique sites for EBV infection and subsequent sequelae. Additionally, the specific site within HLA-DQ determined to be essential for EBV entry is homologous to a site within MHC class I shown by structural studies to bind to the C type-lectin-like natural killer receptor, providing insight into the biochemical nature of the gp42-HLA class II interaction.

Alleles↗
PubMed2000

Epstein-Barr virus entry utilizing HLA-DP or HLA-DQ as a coreceptor.

Epstein-Barr virus (EBV) glycoprotein gp350/gp220 association with cellular CD21 facilitates virion attachment to B lymphocytes. Membrane fusion requires the additional interaction between virion gp42 and cellular HLA-DR. This binding is thought to catalyze membrane fusion through a further association with the gp85-gp25 (gH-gL) complex. Cell lines expressing CD21 but lacking expression of HLA class II molecules are resistant to infection by a recombinant EBV expressing enhanced green fluorescent protein. Surface expression of HLA-DR, HLA-DP, or HLA-DQ confers susceptibility to EBV infection on resistant cells that express CD21. Therefore, HLA-DP or HLA-DQ can substitute for HLA-DR and serve as a coreceptor in EBV entry.

Cell Line↗