CD46 Is a Cellular Receptor for Bovine Viral Diarrhea Virus

Maurer, Karin; Krey, Thomas; Moennig, V.; Thiel, Heinz-Jürgen; Rümenapf, Till

doi:10.1128/jvi.78.4.1792-1799.2004

Cited by 118 publications

(125 citation statements)

References 37 publications

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“…The FLAG epitope was detected with monoclonal antibody M2 (anti-FLAG) from Sigma. Immunoblot analysis of bacterial lysates or CSFV-infected cells was done essentially as described elsewhere (6). Peroxidase-conjugated anti-rabbit-or anti-mouse secondary antibodies were from Dianova.…”

Section: Methodsmentioning

confidence: 99%

Core Protein of Pestiviruses Is Processed at the C Terminus by Signal Peptide Peptidase

Heimann

Sosa

Martoglio

et al. 2006

J Virol

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The core protein of pestiviruses is released from the polyprotein by viral and cellular proteinases. Here we report on an additional intramembrane proteolytic step that generates the C terminus of the core protein. C-terminal processing of the core protein of classical swine fever virus (CSFV) was blocked by the inhibitor (Z-LL) 2 -ketone, which is specific for signal peptide peptidase (SPP). The same effect was obtained by overexpression of the dominant-negative SPP D 265 A mutant. The presence of (Z-LL) 2 -ketone reduced the viability of CSFV almost 100-fold in a concentration-dependent manner. Reduction of virus viability was also observed in infection experiments using a cell line that inducibly expressed SPP D 265 A. The position of SPP cleavage was determined by C-terminal sequencing of core protein purified from virions. The C terminus of CSFV core protein is alanine 255 and is located in the hydrophobic center of the signal peptide. The intramembrane generation of the C terminus of the CSFV core protein is almost identical to the processing scheme of the core protein of hepatitis C viruses.Pestiviruses are small, enveloped RNA viruses that account for important diseases in farm animals, e.g., classical swine fever (also known as hog cholera) and bovine viral diarrhea. Pestiviruses constitute one genus within the Flaviviridae and contain a message sense RNA of about 12.3 kilobases. The genome is translated into a single polyprotein that is processed by cellular and viral proteases into 12 mature proteins. The virion consists of four structural proteins, the core protein and the glycoproteins E rns , E1, and E2 (19). The core protein of all members of the Flaviviridae is a small protein rich in basic amino acids and locates at or near the N terminus of the polyprotein (11). In the pestivirus polyprotein, the core protein is located between the N-terminal protease N pro and the glycoprotein E rns . N pro generates the N terminus (Ser 169 ) of the core protein by autocatalytic cleavage of the polyprotein (15, 18). Core protein is followed by E rns , whose N terminus (Asp 268 ) is generated by signal peptidase (signalase, or SP) (16).Two different mechanisms of release of core protein from the polyprotein have been described for members of the Flaviviridae. Members of the genus Flavivirus (e.g., yellow fever virus [YFV]) employ the virally encoded NS2B-3 protease to generate the C terminus of core protein. The NS2B-3 protease of YFV cleaves the core protein precursor at a tribasic consensus sequence at the N terminus of the preM signal peptide (1). For hepatitis C virus (HCV), signal peptide peptidase (SPP) was recently determined to cleave within the C-terminal domain of core protein (7). Thus far, three different C termini have been proposed for HCV core protein. N-terminal sequencing of HCV core-dihydrofolate reductase fusion proteins revealed cleavage after Leu 179 or Leu 182 (4). In a recent report, Phe 177 was identified as the C terminus of HCV core protein by using matrix-assisted laser desorption ion...

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Section: Methodsmentioning

confidence: 99%

Core Protein of Pestiviruses Is Processed at the C Terminus by Signal Peptide Peptidase

Heimann

Sosa

Martoglio

et al. 2006

J Virol

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“…BVDV receptors include CD46 (22) and low-density-lipoprotein receptor (1). Because of their similarity to flaviviruses, pestiviruses are thought to enter target cells by receptor-mediated endocytosis and acid-triggered fusion of their envelope with an endosomal membrane (1,22). However, BVDV is also known to be resistant to acidic treatments (9,19), a condition often found in viruses with pHindependent entry.…”

mentioning

confidence: 99%

“…Their binding to target cells involves envelope glycoproteins E rns and E2 (16,20,27,33) through interactions with glycosaminoglycans (17,18) and membrane proteins (28,35), respectively. BVDV receptors include CD46 (22) and low-density-lipoprotein receptor (1). Because of their similarity to flaviviruses, pestiviruses are thought to enter target cells by receptor-mediated endocytosis and acid-triggered fusion of their envelope with an endosomal membrane (1,22).…”

mentioning

confidence: 99%

Bovine Viral Diarrhea Virus Entry Is Dependent on Clathrin-Mediated Endocytosis

Lecot

Belouzard

Dubuisson

et al. 2005

J Virol

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Cellular mechanisms of bovine viral diarrhea virus (BVDV) entry in MDBK cells were investigated. Chloroquine, bafilomycin A1, or ammonium chloride inhibited BVDV infection, indicating that an acidic endosomal pH is required for BVDV entry. The tyrosine kinase inhibitor genistein partially inhibited BVDV infection at a postentry step, whereas BVDV entry was strongly inhibited by chlorpromazine or by the overexpression of a dominant-negative form of EPS15, a protein essential for the formation of clathrin-coated vesicles at the plasma membrane. Together, these data indicate that BVDV infection requires an active clathrin-dependent endocytic pathway.

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“…This RNA-polymerase contains a GDD (Glycine-D-aspartate-D-aspartate) active site motif, otherwise known as the motif c [108]. The binding and entry of pestiviruses is a multistep process involving initial attachment of virions, interaction with specific receptor(s), internalization, and membrane fusion [109,110,111,112]. The surface protein CD46 was proposed as receptor for BVDV [104].…”

Section: A Few Salient Features Of the Structure Composition And Funmentioning

confidence: 99%

An Overview of the Immune Evasion Strategies Adopted by Different Viruses with Special Reference to Classical Swine Fever Virus

Chakraborty¹,

Veeregowda²,

Deb³

et al. 2013

Viral Replication

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CD46 Is a Cellular Receptor for Bovine Viral Diarrhea Virus

Cited by 118 publications

References 37 publications

Core Protein of Pestiviruses Is Processed at the C Terminus by Signal Peptide Peptidase

Core Protein of Pestiviruses Is Processed at the C Terminus by Signal Peptide Peptidase

Bovine Viral Diarrhea Virus Entry Is Dependent on Clathrin-Mediated Endocytosis

An Overview of the Immune Evasion Strategies Adopted by Different Viruses with Special Reference to Classical Swine Fever Virus

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