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Infection and Immunity, January 2006, p. 566-577, Vol. 74, No. 1
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.1.566-577.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Identification of the Insulin-Like Growth Factor II Receptor as a Novel Receptor for Binding and Invasion by Listeria monocytogenes

Discipline of Immunology & Microbiology, School of Biomedical Sciences, Faculty of Health, The University of Newcastle, Newcastle, Australia,¹ Vaccines, Immunology/Infection, Viruses and Asthma Group, The Hunter Medical Research Institute, Newcastle, Australia,² Environmental & Life Sciences, Faculty of Science & Mathematics, The University of Newcastle, Newcastle, Australia³

Received 15 April 2005/ Returned for modification 16 June 2005/ Accepted 20 October 2005

The gram-positive bacterium Listeria monocytogenes causes a life-threatening disease known as listeriosis. The mechanism by which L. monocytogenes invades mammalian cells is not fully understood, but the processes involved may provide targets to prevent and treat listeriosis. Here, for the first time, we have identified the insulin-like growth factor II receptor (IGFIIR; also known as the cation-independent mannose 6-phosphate receptor ^CIM6PR or CD222) as a novel receptor for binding and invasion of Listeria species. Random peptide phage display was employed to select a peptide sequence by panning with immobilized L. monocytogenes cells; this peptide sequence corresponds to a sequence within the mannose 6-phosphate binding site of the IGFIIR. All Listeria spp. specifically bound the labeled peptide but not a control peptide, which was demonstrated using fluorescence spectrophotometry and fluorescence-activated cell sorting. Further evidence for binding of the receptor by L. monocytogenes and L. innocua was provided by affinity purification of the bovine IGFIIR from fetal calf serum by use of magnetic beads coated with cell preparations of Listeria spp. as affinity matrices. Adherence to and invasion of mammalian cells by L. monocytogenes was significantly inhibited by both the synthetic peptide and mannose 6-phosphate but not by appropriate controls. These observations indicate a role for the IGFIIR in the adherence and invasion of L. monocytogenes of mammalian cells, perhaps in combination with known mechanisms. Ligation of IGFIIR by L. monocytogenes may be a novel mechanism that contributes to the regulation of infectivity, possibly in combination with other mechanisms.

Editor: J. F. Urban, Jr.