The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex.
Human cytomegalovirus (HCMV) forms two gH/gL glycoprotein complexes, gH/gL/gO and gH/gL/pUL(128,130,131A), which determine the tropism, the entry pathways and the mode of spread of the virus. For murine cytomegalovirus (MCMV), which serves as a model for HCMV, a gH/gL/gO complex functionally homolog...
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oai:doaj.org-article:6ec46bf2081f4bc6bd859ac26f166b542021-11-18T06:07:52ZThe viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex.1553-73661553-737410.1371/journal.ppat.1003493https://doaj.org/article/6ec46bf2081f4bc6bd859ac26f166b542013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23935483/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Human cytomegalovirus (HCMV) forms two gH/gL glycoprotein complexes, gH/gL/gO and gH/gL/pUL(128,130,131A), which determine the tropism, the entry pathways and the mode of spread of the virus. For murine cytomegalovirus (MCMV), which serves as a model for HCMV, a gH/gL/gO complex functionally homologous to the HCMV gH/gL/gO complex has been described. Knock-out of MCMV gO does impair, but not abolish, virus spread indicating that also MCMV might form an alternative gH/gL complex. Here, we show that the MCMV CC chemokine MCK-2 forms a complex with the glycoprotein gH, a complex which is incorporated into the virion. We could additionally show that mutants lacking both, gO and MCK-2 are not able to produce infectious virus. Trans-complementation of these double mutants with either gO or MCK-2 showed that both proteins can promote infection of host cells, although through different entry pathways. MCK-2 has been extensively studied in vivo by others. It has been shown to be involved in attracting cells for virus dissemination and in regulating antiviral host responses. We now show that MCK-2, by forming a complex with gH, strongly promotes infection of macrophages in vitro and in vivo. Thus, MCK-2 may play a dual role in MCMV infection, as a chemokine regulating the host response and attracting specific target cells and as part of a glycoprotein complex promoting entry into cells crucial for virus dissemination.Felicia M WagnerIlija BrizicAdrian PragerTihana TrsanMaja ArapovicNiels A W LemmermannJürgen PodlechMatthias J ReddehaseFrederic LemnitzerJens Bernhard BosseMartina GimpflLisa MarcinowskiMargaret MacDonaldHeiko AdlerUlrich H KoszinowskiBarbara AdlerPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 7, p e1003493 (2013) |
| institution |
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| collection |
DOAJ |
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| topic |
Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 |
| spellingShingle |
Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Felicia M Wagner Ilija Brizic Adrian Prager Tihana Trsan Maja Arapovic Niels A W Lemmermann Jürgen Podlech Matthias J Reddehase Frederic Lemnitzer Jens Bernhard Bosse Martina Gimpfl Lisa Marcinowski Margaret MacDonald Heiko Adler Ulrich H Koszinowski Barbara Adler The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex. |
| description |
Human cytomegalovirus (HCMV) forms two gH/gL glycoprotein complexes, gH/gL/gO and gH/gL/pUL(128,130,131A), which determine the tropism, the entry pathways and the mode of spread of the virus. For murine cytomegalovirus (MCMV), which serves as a model for HCMV, a gH/gL/gO complex functionally homologous to the HCMV gH/gL/gO complex has been described. Knock-out of MCMV gO does impair, but not abolish, virus spread indicating that also MCMV might form an alternative gH/gL complex. Here, we show that the MCMV CC chemokine MCK-2 forms a complex with the glycoprotein gH, a complex which is incorporated into the virion. We could additionally show that mutants lacking both, gO and MCK-2 are not able to produce infectious virus. Trans-complementation of these double mutants with either gO or MCK-2 showed that both proteins can promote infection of host cells, although through different entry pathways. MCK-2 has been extensively studied in vivo by others. It has been shown to be involved in attracting cells for virus dissemination and in regulating antiviral host responses. We now show that MCK-2, by forming a complex with gH, strongly promotes infection of macrophages in vitro and in vivo. Thus, MCK-2 may play a dual role in MCMV infection, as a chemokine regulating the host response and attracting specific target cells and as part of a glycoprotein complex promoting entry into cells crucial for virus dissemination. |
| format |
article |
| author |
Felicia M Wagner Ilija Brizic Adrian Prager Tihana Trsan Maja Arapovic Niels A W Lemmermann Jürgen Podlech Matthias J Reddehase Frederic Lemnitzer Jens Bernhard Bosse Martina Gimpfl Lisa Marcinowski Margaret MacDonald Heiko Adler Ulrich H Koszinowski Barbara Adler |
| author_facet |
Felicia M Wagner Ilija Brizic Adrian Prager Tihana Trsan Maja Arapovic Niels A W Lemmermann Jürgen Podlech Matthias J Reddehase Frederic Lemnitzer Jens Bernhard Bosse Martina Gimpfl Lisa Marcinowski Margaret MacDonald Heiko Adler Ulrich H Koszinowski Barbara Adler |
| author_sort |
Felicia M Wagner |
| title |
The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex. |
| title_short |
The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex. |
| title_full |
The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex. |
| title_fullStr |
The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex. |
| title_full_unstemmed |
The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex. |
| title_sort |
viral chemokine mck-2 of murine cytomegalovirus promotes infection as part of a gh/gl/mck-2 complex. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2013 |
| url |
https://doaj.org/article/6ec46bf2081f4bc6bd859ac26f166b54 |
| work_keys_str_mv |
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