Antigenic Determinants of Infective and Inactivated Human Rhinovirus Type 2

Abstract

Treatment of human rhinovirus type 2 (HRV 2) virions at pH 5, at 56 C or in 2 M urea, produces one or both of two types of subviral particles. These subviral particles sediment at 135S or at 80S and both share what have been designated as C-antigenic determinants; the determinants of native virions have been designated D. These sets of determinants have been contrasted by the techniques of immunodiffusion, complement fixation, and serum blocking, and the results indicate that many or most of the D-determinants are lost in the conversion to C antigenicity. Some of the HRV 2 C-determinants also react, in immunodiffusion and in complement fixation tests, with antisera produced against HRV 1A virions. The inverse reaction has also been detected by complement fixation. Purified natural top component (NTC) of HRV 2 contains C-and, to a lesser extent, D-determinants. The D-determinants of NTC are also, like those of virions, lost upon treatment at pH 5. These results are discussed in terms of a conformational model for the Dto C-antigenic conversion.

Characterization of rhinovirus subviral A particles via capillary electrophoresis, electron microscopy and gas‐phase electrophoretic mobility molecular analysis: Part I

“…It is of note that 135S particles prepared according to ref. [2] exhibited an electrophoretic net mobility = −16.6 × 10 −9 m 2 /Vs (Table 1) in CE, a value in good accordance with the electrophoretic net mobility of AI particles as stated above. However, our initial experiments demonstrated that incubation at 56ЊC for 10 min (Fig.…”

Characterization of rhinovirus subviral A particles via capillary electrophoresis, electron microscopy and gas phase electrophoretic mobility molecular analysis: Part II

“…In the course of the present manuscript we focused on AI intermediates. From the sum of the experimental results concerning the particle composition we find AI particles of our research work indistinguishable from subviral A particles of rhinovirus uncoating as previously described [2]. Additional experiments targeted possible factors influencing the formation of intermediate AI particles as well as its antigenicity.…”

“…After spin SEC, the electropherogram allows the conclusion that AI particles possess indeed only three viral proteins (VPs): VP4 from the virion is missing (dashed line, highlighted area). This together with detected RNA allows the conclusion that intermediate AI particles are identical with 135S intermediates as described in 1973 by Lonberg-Holm and Yin [2]. Injection and electrophoresis were as in Fig.…”

“…Concerning the composition of AI particles, we found that they consist of three (instead of four as found for intact virions) VPs -VP4 is missing -and still contained a bulk of approximately 93% of the viral RNA genome in average. So, we could demonstrate that AI particles correspond to subviral 135S particles as described by Lonberg-Holm and Yin [2]. However, small parts of the RNA are seemingly protruding out of the viral capsid already at this intermediate stage as can be learned from experiments in the presence of RNase inhibitor, which yielded subviral assemblies with electrophoretic mobilities closer to values for free RNA.…”

Isolation and antigenic characterization of dense particles of swine enteroviruses.

“…These non-infectious particles which lack the VP4 polypeptide can also be obtained by in vitro treatment of the virion with acid, alkali, heat or urea (Lonberg-Holm and Yin, 1973). As most of the properties of "A particles" are very similar to those of the dense particles reported here, dense partides may be equivalent to "A particles".…”