Received by Qing
Received on 2014-10-29
ID No. APJTD-2014-0260
First revised on
Second revised on
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埃博拉 GP-F88A 突变引起的次生结构无结构改变
No conformation change of secondary structure due to Ebola GP-F88A mutation
Beuy Joob1
1. Sanitation 1 Medical Academic Center, Bangkok Thailand
Viroj Wiwanitkit2
2. Visiting professor, Hainan Medical University, China
Correspondence
Beuy Joob
Sanitation 1 Medical Academic Center, Bangkok Thailand
Email: beuyjoob@hotmail.com
Dear editor, the Ebola virus outbreak is the serious problem at present. An interesting concern
is on the mutation of the virus that might lead to alteration of clinical pattern. An interesting
reported mutation is the F88A mutation of Ebola viral glycoprotein. Martinez et al. reported
that this mutation could restrict viral entry in a host species- and cell-type-specific manner
[1]. Basically, the sense mutation might cause a change in conformation due to secondary
structure aberration. For the mentioned F88A mutation, it is still no data on the resulted
structural aberration. Here, the authors tried to predict the secondary structure change due to
the mutation. The standard bioinformatics analysis (APSSP2 [2]) was done and the result
showed no secondary structure change due to the mutation (Figure 1). This method is
confirmed for efficacy and used in previous published paper by Zhou et al [3]. The position
88 still preserved “coil” appearance in both wild and mutated (F88A) type of Ebola viral
glycoprotein. This can imply that the observed clinical pattern alteration by Martinez et al.
should not be due to the alteration of secondary structure.
References
1. Martinez O, Ndungo E, Tantral L, Miller EH, Leung LW, Chandran K, Basler CF. A
mutation in the Ebola virus envelope glycoprotein restricts viral entry in a host
species- and cell-type-specific manner. J Virol. 2013 Mar;87(6):3324-34.
2. Raghava GPS. APSSP2 : A combination method for protein secondary structure
prediction based on neural network and example based learning. CASP5.2002: A-132.
3. Zhou HZ, Xu HF, Xin XM, Guan XR, Zhou J. Position 22 of the V3 loop is
associated with co-receptor usage and disease progression in HIV-1 subtype B
isolates. Curr HIV Res. 2011 Dec 1;9(8):636-41.
Figure 1. The predicted secondary structure in wild and mutated (F88A) showing the
position 82 – 95 (H = helix, C = coil).
Wild
Mutated
KH
RC
WC
GH
AH
RH
SC
GC
VC
PC
PC
KC
VC
VC
KH
RC
WC
GC
FC
RC
SC
GC
VC
PC
PC
KC
VC
VC
secondary
Wild Mutated 88 --- coil