Functional studies of host-specific ephrin-B ligands as Henipavirus receptors.
Hendra virus (HeV) and Nipah virus (NiV) are closely related paramyxoviruses that infect and cause disease in a wide range of mammalian hosts. To determine whether host receptor molecules play a role in species-specific and/or virus-specific infection we have cloned and characterized ephrin-B2 and ephrin-B3 ligands from a range of species, including human, horse, pig, cat, dog, bats (Pteropus alecto and Pteropus vampyrus) and mouse. HeV and NiV were both able to infect cells expressing any of the ephrin-B2 and ephrin-B3 molecules. There did not appear to be significant differences in receptor function from different species or receptor usage by HeV and NiV. Soluble ephrin ligands, their receptors and G-specific human monoclonal antibodies differentially blocked henipavirus infections suggesting different receptor affinities, overlapping receptor binding domains of the henipavirus attachment glycoprotein (G) and that the functional domains of the ephrin ligands may be important for henipavirus binding.
CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, Victoria 3220, Australia. Katharine.Bossart@csiro.au
Katharine N
KN
Bossart
Mary
M
Tachedjian
Jennifer A
JA
McEachern
Gary
G
Crameri
Zhongyu
Z
Zhu
Dimiter S
DS
Dimitrov
Christopher C
CC
Broder
Lin-Fa
LF
Wang
D000595:Amino Acid Sequence; D000818:Animals; D000914:Antibodies, Viral; D001665:Binding Sites; D002460:Cell Line; D002478:Cells, Cultured; D003001:Cloning, Molecular; D004247:DNA; D036388:Ephrin-B2 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D036389:Ephrin-B3 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D045403:Henipavirus / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D011991:Receptors, Virus / Q000378:metabolism*; D013045:Species Specificity
D000914:Antibodies, Viral; D036388:Ephrin-B2; D036389:Ephrin-B3; D008024:Ligands; D011991:Receptors, Virus; D004247:DNA