Structural Studies on Virus-Antibody Complexes

As of a decade ago, most of our structural information about antibody-virus interactions was limited to influenzavirus. Since then, there has been a flurry of structural studies aimed at elucidating the mechanism of 

Influenzavirus studies were the first to examine interactions between viral proteins and antibodies. From this work, ideas started to develop about methods viruses have evolved to avoid immune surveillance. 

Influenza is an infection of the respiratory tract caused by the influenzavirus. Compared with most other viral respiratory infections, such as the common cold, influenza infection often causes a more severe illness. In an average year, influenza is associated with more than 20,000 deaths nationwide and more than 100,000 hospitalizations. Influenza-viruses are divided into three types designated A, B, and C. Influenza types A and B are responsible for epidemics of respiratory illness that occur almost every winter and are often associated with increased rates for hospitalization and death. Type C infection usually causes either a mild respiratory illness or no symptoms at all [16]. 

When the high-resolution structure of influenza virus N9 neuraminidase (NA) was determined, it was noted that the conserved residues involved in sialic acid binding were located in a crevasse [17]. Residues within this deep depression are conserved whereas the residues about the rim vary with serotype. This suggests that conserved residues are hidden from antibody recognition. The authors suggested that such architecture might 

The study by Prasad et al. [21] represented the first visualization of an intact virion complexed with neutralizing antibodies. The success of this work had tremendous impact on the studies that followed. 

---