A Single Amino Acid Change in the Cytoplasmic Domains of Measles Virus Glycoproteins H and F Alters Targeting, Endocytosis, and Cell Fusion in Polarized Madin-Darby Canine Kidney Cells

Moll, Markus; Klenk, Hans‐Dieter; Herrler, Georg; Maisner, Andrea

doi:10.1074/jbc.m010183200

Cited by 52 publications

(45 citation statements)

References 44 publications

(35 reference statements)

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“…Various evidence has been accumulated indicating that subtle differences in the envelope proteins of MV can play a role in altering the tropism, virus uptake, cell-to-cell fusion and pathogenicity (Bartz et al, 1996;Bieback et al, 2002;Hsu et al, 1998;Johnston et al, 1999;Lecouturier et al, 1996;Moeller et al, 2001;Moll et al, 2001;Ohgimoto et al, 2001;Plemper et al, 2002;Shibahara et al, 1994;Takeuchi et al, 2002). To investigate the molecular basis for the differential spread of MV wild-types in cultures of HUVECs, we will further analyse the sequences of the envelope genes of the MV wildtypes and intend functional studies with corresponding recombinant viruses.…”

Section: Discussionmentioning

confidence: 99%

CD46- and CD150-independent endothelial cell infection with wild-type measles viruses

Andrés¹,

Obojes²,

Kim

et al. 2003

Journal of General Virology

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Measles virus (MV) infects endothelial cells of the skin, the brain and other organs during acute or persistent infections. Endothelial cells are supposed to play an important role in virus spread from the blood stream to surrounding tissues. CD46 and CD150 (signalling lymphocytic activation molecule, SLAM) have been described as cellular receptors for certain MV strains. We found that human umbilical vein and brain microvascular endothelial cells (HUVECs and HBMECs) were CD46-positive, but did not express SLAM. Wild-type MV strains, which do not use CD46 as a receptor at the surface of transfected Chinese hamster ovary cells, infected HUVECs and HBMECs to varying extents in a strain-dependent way. This infection was not inhibited by antibodies to CD46. These data suggest the presence of an additional unidentified receptor for MV uptake and spread in human endothelial cells. INTRODUCTIONAfter acute infection of the upper respiratory tract, measles virus (MV) is rapidly transported to draining lymph nodes forming giant cells in the reticulo-endothelial system. MV then establishes a systemic infection and spreads to different organs, including the skin. In these organs, virus replicates primarily in endothelial cells (ECs), epithelial cells and monocytes/macrophages (Griffin & Bellini, 1996). ECs of dermal capillaries (Kimura et al., 1975) and small vessels throughout the body show clear evidence of MV infection. This appears to play a central role in pathogenesis, leading to changes in the skin, conjunctivae, mucous membranes and the brain (Cosby & Brankin, 1995), accompanied by vascular dilatation, increased vascular permeability, mononuclear cell infiltration and infection of surrounding tissues. In rare cases, the EC infection may extend to a severe haemorrhagic infection with confluent haemorrhagic skin eruptions and intravascular coagulopathy, so-called haemorrhagic or black measles. Brain ECs and capillary endothelium of lymph nodes and the thymus have been found to be infected in fatal cases of acute measles (Esolen et al., 1995; Moench et al., 1988). In subacute sclerosing panencephalitis (SSPE) patients, brain ECs appear to be infected in addition to various neural cells (Allen et al., 1996;Isaacson et al., 1996;Kirk et al., 1991).Following the identification of CD46 as a receptor for MV vaccine and laboratory strains (Dörig et al., 1993;Naniche et al., 1993a), evidence has accumulated that many wildtype isolates do not use CD46 as a receptor. Recently, the signalling lymphocytic activation molecule (SLAM, CD150) has been identified as a common receptor interacting with MV vaccine as well as wild-type strains (Erlenhoefer et al., 2001(Erlenhoefer et al., , 2002Hsu et al., 2001; Ono et al., 2001a, b;Tatsuo et al., 2000). SLAM is expressed on human B cell lines, primary activated B and T cells, memory cells and activated monocytes and monocyte-derived dendritic cells (Cocks et al., 1995;Minagawa et al., 2001;Ohgimoto et al., 2001;Polacino et al., 1996;Punnonen et al., 1997), and its usage as a receptor c...

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Section: Discussionmentioning

confidence: 99%

CD46- and CD150-independent endothelial cell infection with wild-type measles viruses

Andrés¹,

Obojes²,

Kim

et al. 2003

Journal of General Virology

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“…1) has been described previously (15). The F gene of the measles virus (MV) Edmonston strain was cloned into the pCG vector (16). Amersham Biosciences) at a final concentration of 100 Ci/ml for 10 min.…”

Section: Methodsmentioning

confidence: 99%

The Nipah Virus Fusion Protein Is Cleaved within the Endosomal Compartment

Diederich

Moll

Klenk

et al. 2005

Journal of Biological Chemistry

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Nipah virus (NiV) is a recently emerged and highly pathogenic paramyxovirus that causes a systemic infection in animals and humans and can infect a wide range of cultured cells. Interestingly, the NiV fusion (F) protein has a single arginine at the cleavage site similar to paramyxoviruses that are activated by exogenous trypsin-like enzymes only present in specific cells and tissues and therefore only cause localized infections. We show here that NiV F activation is not mediated by an exogenous serum protease but by an endogenous ubiquitous cellular protease after endocytosis of the protein.In addition to endocytosis, acidification of the endosome is a prerequisite for F cleavage. These results show that activation of the NiV F protein depends on a type of proteolytic cleavage that is clearly different from what is known for other paramyxoviral and orthomyxoviral fusion proteins. To our knowledge, this is the first example of a viral class I fusion protein whose activation depends on clathrin-mediated constitutive endocytosis.

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“…Some early studies of henipavirus fusion demonstrated that the homologous HeV glycoproteins fuse more efficiently than the NiV glycoproteins (Bossart et al, 2002), but it has not been clear why this is the case. Since CDV and NiV attachment protein mutants with cytoplasmic domains of 15 residues or fewer lack tyrosine motifs important for post-translational sorting to the basolateral surface of polarized cells (Moll et al, 2001;Runkler et al, 2009;Weise et al, 2010), the resulting loss of appropriate intracellular transport likely disrupts protein homeostasis and decreases protein expression levels.…”

Section: Disruption Of Niv G Cytoplasmic Signalling Motifs Decreases mentioning

confidence: 99%

Morbillivirus and henipavirus attachment protein cytoplasmic domains differently affect protein expression, fusion support and particle assembly

Sawatsky

Bente

Czub

et al. 2016

Journal of General Virology

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The amino-terminal cytoplasmic domains of paramyxovirus attachment glycoproteins include trafficking signals that influence protein processing and cell surface expression. To characterize the role of the cytoplasmic domain in protein expression, fusion support and particle assembly in more detail, we constructed chimeric Nipah virus (NiV) glycoprotein (G) and canine distemper virus (CDV) haemagglutinin (H) proteins carrying the respective heterologous cytoplasmic domain, as well as a series of mutants with progressive deletions in this domain. CDV H retained fusion function and was normally expressed on the cell surface with a heterologous cytoplasmic domain, while the expression and fusion support of NiV G was dramatically decreased when its cytoplasmic domain was replaced with that of CDV H. The cell surface expression and fusion support functions of CDV H were relatively insensitive to cytoplasmic domain deletions, while short deletions in the corresponding region of NiV G dramatically decreased both. In addition, the first 10 residues of the CDV H cytoplasmic domain strongly influence its incorporation into virus-like particles formed by the CDV matrix (M) protein, while the co-expression of NiV M with NiV G had no significant effect on incorporation of G into particles. The cytoplasmic domains of both the CDV H and NiV G proteins thus contribute differently to the virus life cycle.

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A Single Amino Acid Change in the Cytoplasmic Domains of Measles Virus Glycoproteins H and F Alters Targeting, Endocytosis, and Cell Fusion in Polarized Madin-Darby Canine Kidney Cells

Cited by 52 publications

References 44 publications

CD46- and CD150-independent endothelial cell infection with wild-type measles viruses

CD46- and CD150-independent endothelial cell infection with wild-type measles viruses

The Nipah Virus Fusion Protein Is Cleaved within the Endosomal Compartment

Morbillivirus and henipavirus attachment protein cytoplasmic domains differently affect protein expression, fusion support and particle assembly

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