Genetic analysis and antigenic characterization of human respiratory syncytial virus group A viruses isolated in Germany 1996–2008

Virus Genes ◽  
2013 ◽  
Vol 47 (2) ◽  
pp. 210-218 ◽  
Author(s):  
Ortwin Adams ◽  
Judith Werzmirzowsky ◽  
Hartmut Hengel
2005 ◽  
Vol 77 (2) ◽  
pp. 311-316 ◽  
Author(s):  
Mónica C. Galiano ◽  
Vivian Luchsinger ◽  
Cristina M. Videla ◽  
Leila De Souza ◽  
Silvia Sánchez Puch ◽  
...  

2006 ◽  
Vol 37 (4) ◽  
pp. 543-547 ◽  
Author(s):  
Clara Savón ◽  
Angel Goyenechea ◽  
Odalys Valdés ◽  
José Aguilar ◽  
Grehete González ◽  
...  

2017 ◽  
Vol 91 (13) ◽  
Author(s):  
Normand Blais ◽  
Martin Gagné ◽  
Yoshitomo Hamuro ◽  
Patrick Rheault ◽  
Martine Boyer ◽  
...  

ABSTRACT The human respiratory syncytial virus (hRSV) fusion (F) protein is considered a major target of the neutralizing antibody response to hRSV. This glycoprotein undergoes a major structural shift from the prefusion (pre-F) to the postfusion (post-F) state at the time of virus-host cell membrane fusion. Recent evidences suggest that the pre-F state is a superior target for neutralizing antibodies compared to the post-F state. Therefore, for vaccine purposes, we have designed and characterized a recombinant hRSV F protein, called Pre-F-GCN4t, stabilized in a pre-F conformation. To show that Pre-F-GCN4t does not switch to a post-F conformation, it was compared with a recombinant post-F molecule, called Post-F-XC. Pre-F-GCN4t was glycosylated and trimeric and displayed a conformational stability different from that of Post-F-XC, as shown by chemical denaturation. Electron microscopy analysis suggested that Pre-F-GCN4t adopts a lollipop-like structure. In contrast, Post-F-XC had a typical elongated conical shape. Hydrogen/deuterium exchange mass spectrometry demonstrated that the two molecules had common rigid folding core and dynamic regions and provided structural insight for their biophysical and biochemical properties and reactivity. Pre-F-GCN4t was shown to deplete hRSV-neutralizing antibodies from human serum more efficiently than Post-F-XC. Importantly, Pre-F-GCN4t was also shown to bind D25, a highly potent monoclonal antibody specific for the pre-F conformation. In conclusion, this construct presents several pre-F characteristics, does not switch to the post-F conformation, and presents antigenic features required for a protective neutralizing antibody response. Therefore, Pre-F-GCN4t can be considered a promising candidate vaccine antigen. IMPORTANCE Human respiratory syncytial virus (RSV) is a global leading cause of infant mortality and adult morbidity. The development of a safe and efficacious RSV vaccine remains an important goal. The RSV class I fusion (F) glycoprotein is considered one of the most promising vaccine candidates, and recent evidences suggest that the prefusion (pre-F) state is a superior target for neutralizing antibodies. Our study presents the physicochemical characterization of Pre-F-GCN4t, a molecule designed to be stabilized in the pre-F conformation. To confirm its pre-F conformation, Pre-F-GCN4t was analyzed in parallel with Post-F-XC, a molecule in the post-F conformation. Our results show that Pre-F-GCN4t presents characteristics of a stabilized pre-F conformation and support its use as an RSV vaccine antigen. Such an antigen may represent a significant advance in the development of an RSV vaccine.


2013 ◽  
pp. n/a-n/a ◽  
Author(s):  
Hiroyuki Tsukagoshi ◽  
Hajime Yokoi ◽  
Miho Kobayashi ◽  
Izumi Kushibuchi ◽  
Reiko Okamoto-Nakagawa ◽  
...  

Heliyon ◽  
2019 ◽  
Vol 5 (3) ◽  
pp. e01394
Author(s):  
Vitor Brassolatti Machado ◽  
Jéssica Maróstica de Sá ◽  
Ana Karla Miranda Prado ◽  
Karina Alves de Toledo ◽  
Luis Octávio Regasini ◽  
...  

2019 ◽  
Vol 71 ◽  
pp. 166-178 ◽  
Author(s):  
Somayeh Shatizadeh Malekshahi ◽  
Shaghayegh Razaghipour ◽  
Yazdan Samieipoor ◽  
Farhad B. Hashemi ◽  
Ali Akbar Rahbari Manesh ◽  
...  

2016 ◽  
Vol 89 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Swati Saxena ◽  
Dharamveer Singh ◽  
Amreen Zia ◽  
Jyoti Umrao ◽  
Naveen Srivastava ◽  
...  

2007 ◽  
Vol 88 (10) ◽  
pp. 2719-2723 ◽  
Author(s):  
Sheng-Jiun Wu ◽  
Albert Schmidt ◽  
Eric J. Beil ◽  
Nicole D. Day ◽  
Patrick J. Branigan ◽  
...  

Chimeric 101F (ch101F) is a mouse–human chimeric anti-human respiratory syncytial virus (HRSV) neutralizing antibody that recognizes residues within antigenic site IV, V, VI of the fusion (F) glycoprotein. The binding of ch101F to a series of peptides overlapping aa 422–438 spanning antigenic site IV, V, VI was analysed. Residues 423–436 comprise the minimal peptide sequence for ch101F binding. Substitution analysis revealed that R429 and K433 are critical for ch101F binding, whilst K427 makes a minor contribution. Binding of ch101F to a series of single mutations at positions 427, 429 and 433 in the F protein expressed recombinantly on the cell surface confirmed the peptide results. Sequence analysis of viruses selected for resistance to neutralization by ch101F indicated that a single change (K433T) in the F protein allowed ch101F escape. The results confirm that ch101F and palivizumab have different epitope specificity and define key residues for ch101F recognition.


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