Breaking In: Human Metapneumovirus Fusion and Entry
Human metapneumovirus (HMPV) is a leading cause of respiratory infection that causes upper airway and severe lower respiratory tract infections. HMPV infection is initiated by viral surface glycoproteins that attach to cellular receptors and mediate virus membrane fusion with cellular membranes. Mos...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2013-01-01
|
| Series: | Viruses |
| Subjects: | |
| Online Access: | http://www.mdpi.com/1999-4915/5/1/192 |
| _version_ | 1818163306580410368 |
|---|---|
| author | John V. Williams Reagan G. Cox |
| author_facet | John V. Williams Reagan G. Cox |
| author_sort | John V. Williams |
| collection | DOAJ |
| description | Human metapneumovirus (HMPV) is a leading cause of respiratory infection that causes upper airway and severe lower respiratory tract infections. HMPV infection is initiated by viral surface glycoproteins that attach to cellular receptors and mediate virus membrane fusion with cellular membranes. Most paramyxoviruses use two viral glycoproteins to facilitate virus entry—an attachment protein and a fusion (F) protein. However, membrane fusion for the human paramyxoviruses in the Pneumovirus subfamily, HMPV and respiratory syncytial virus (hRSV), is unique in that the F protein drives fusion in the absence of a separate viral attachment protein. Thus, pneumovirus F proteins can perform the necessary functions for virus entry, i.e., attachment and fusion. In this review, we discuss recent advances in the understanding of how HMPV F mediates both attachment and fusion. We review the requirements for HMPV viral surface glycoproteins during entry and infection, and review the identification of cellular receptors for HMPV F. We also review our current understanding of how HMPV F mediates fusion, concentrating on structural regions of the protein that appear to be critical for membrane fusion activity. Finally, we illuminate key unanswered questions and suggest how further studies can elucidate how this clinically important paramyxovirus fusion protein may have evolved to initiate infection by a unique mechanism. |
| first_indexed | 2024-12-11T16:47:28Z |
| format | Article |
| id | doaj.art-6d545b7b6ed14feeaab98f07ab79d636 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-12-11T16:47:28Z |
| publishDate | 2013-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-6d545b7b6ed14feeaab98f07ab79d6362022-12-22T00:58:10ZengMDPI AGViruses1999-49152013-01-015119221010.3390/v5010192Breaking In: Human Metapneumovirus Fusion and EntryJohn V. WilliamsReagan G. CoxHuman metapneumovirus (HMPV) is a leading cause of respiratory infection that causes upper airway and severe lower respiratory tract infections. HMPV infection is initiated by viral surface glycoproteins that attach to cellular receptors and mediate virus membrane fusion with cellular membranes. Most paramyxoviruses use two viral glycoproteins to facilitate virus entry—an attachment protein and a fusion (F) protein. However, membrane fusion for the human paramyxoviruses in the Pneumovirus subfamily, HMPV and respiratory syncytial virus (hRSV), is unique in that the F protein drives fusion in the absence of a separate viral attachment protein. Thus, pneumovirus F proteins can perform the necessary functions for virus entry, i.e., attachment and fusion. In this review, we discuss recent advances in the understanding of how HMPV F mediates both attachment and fusion. We review the requirements for HMPV viral surface glycoproteins during entry and infection, and review the identification of cellular receptors for HMPV F. We also review our current understanding of how HMPV F mediates fusion, concentrating on structural regions of the protein that appear to be critical for membrane fusion activity. Finally, we illuminate key unanswered questions and suggest how further studies can elucidate how this clinically important paramyxovirus fusion protein may have evolved to initiate infection by a unique mechanism.http://www.mdpi.com/1999-4915/5/1/192metapneumovirusfusion proteinparamyxovirusintegrin |
| spellingShingle | John V. Williams Reagan G. Cox Breaking In: Human Metapneumovirus Fusion and Entry Viruses metapneumovirus fusion protein paramyxovirus integrin |
| title | Breaking In: Human Metapneumovirus Fusion and Entry |
| title_full | Breaking In: Human Metapneumovirus Fusion and Entry |
| title_fullStr | Breaking In: Human Metapneumovirus Fusion and Entry |
| title_full_unstemmed | Breaking In: Human Metapneumovirus Fusion and Entry |
| title_short | Breaking In: Human Metapneumovirus Fusion and Entry |
| title_sort | breaking in human metapneumovirus fusion and entry |
| topic | metapneumovirus fusion protein paramyxovirus integrin |
| url | http://www.mdpi.com/1999-4915/5/1/192 |
| work_keys_str_mv | AT johnvwilliams breakinginhumanmetapneumovirusfusionandentry AT reagangcox breakinginhumanmetapneumovirusfusionandentry |