transcriptional profile of marek’s disease virus genes in chicken thymus during different phases...

BRIEF REPORT

Transcriptional profile of Marek’s disease virus genes in chickenthymus during different phases of MDV infection

Xuming Hu • Aijian Qin • Ji Miao •

Wencai Xu • Chuan Yu • Kun Qian •

Hongxia Shao

Received: 5 November 2012 / Accepted: 5 February 2013 / Published online: 15 March 2013

� Springer-Verlag Wien 2013

Abstract In this study, 86 Marek’s disease virus (MDV)

transcripts were detected in chicken thymus infected with

RB1B strain. Forty-seven of them, which were mainly

involved in viral replication and immune escape, were

detected at 7 days postinfection (dpi). Expression of most

of the genes was increased at 21 and 28 dpi but reduced or

shut down at 14 dpi. Unlike others tissues, we found that a

latent infection was established at 14 dpi in infected thy-

mus. Here, we show the kinetics of expression of MDV

transcripts and their relative expression in infected thymus.

Marek’s disease virus (MDV), genus Mardivirus, species

Gallid herpesvirus 2, induces T lymphomas and nervous

disorders in chickens [2]. The primary target cells for MDV

infection in chickens are B lymphocytes. The virus

destroys cells a few days after infection, but this is then

followed by a latent phase. During latent infection of

activated T cells, genes are expressed at a low level, but the

virus can be recovered from lymphocytes [10]. Only a few

viral genes, such as ICP4, are expressed during latency [4].

These latently infected T lymphocytes are the means of

virus dissemination to the skin and feather follicle epithe-

lial cells. As infection progresses, the late cytolytic phase

and tumour development occur. However, we do not know

whether the progress of the virus infection in the thymus is

the same as in other organs. Recently, the microarray

technique has become a valuable tool for evaluating host

and viral gene expression patterns, but research has mainly

been focused on the spleen [6–8]. There have been no

reports on these expression patterns in chicken thymus, an

important central lymphoid organ.

The thymus is the main organ in which the maturation

and differentiation of avian T lymphocytes take place.

Tumor cells that develop as a result of MDV infection are

T-cells. Therefore, it is important to determine the tran-

scriptional profile of virus genes in MDV-infected chicken

thymus. In addition, the kinetics of expression of MDV

transcripts and their relative abundance during different

infection stages will help us to understand the molecular

pathogenesis of this virus and its interaction with its host in

a natural infection.

In this study, we performed a global gene expression

profiling of MDV in chicken thymus at 7, 14, 21 and 28 dpi

(days postinfection) using Affymetrix GeneChip Chicken

Genome Arrays, which contain most of the known MDV

genes. The thymus samples were from the same chickens

that were used in previously studies [9, 14]. Total RNA

was extracted from the thymus tissues of MDV-infected

birds using TRIzol Reagent (Life Technologies, Carlsbad,

CA, US) following the manufacturer’s instructions, and

RNA integrity was checked using an Agilent Bioanalyzer

2100 (Agilent Technologies, Santa Clara, CA, USA). The

total RNA was then purified using an RNeasy Mini Kit

(QIAGEN, GmBH, Germany) and an RNase-Free DNase

Set (QIAGEN, GmBH, Germany). The RNA amplification

and labelling, array hybridisation and data acquisition were

Electronic supplementary material The online version of thisarticle (doi:10.1007/s00705-013-1665-z) contains supplementarymaterial, which is available to authorized users.

X. Hu � A. Qin (&) � K. Qian � H. Shao

Ministry of Education Key Lab for Avian Preventive Medicine,

Yangzhou University, No. 12 East Wenhui Road, Yangzhou,

Jiangsu 225009, People’s Republic of China

e-mail: [email protected]

A. Qin � J. Miao � W. Xu � C. Yu � K. Qian � H. Shao

Key Laboratory of Jiangsu Preventive Veterinary Medicine,

Yangzhou University, Yangzhou 225009,

People’s Republic of China

123

Arch Virol (2013) 158:1787–1793

DOI 10.1007/s00705-013-1665-z

http://dx.doi.org/10.1007/s00705-013-1665-z

Table 1 Comparative MDV gene expression profile in infected chicken thymus tissue at 7, 14, 21 and 28 dpi

Probe_Set_ID Gene ID Relative expression level Fold change

7 dpi 14 dpi 21 dpi 28 dpi I14/

I7

I21/

I7

I28/

I7

MDV genes and gene products involved in immune evasion, tumor development and/or pathogenesis

AF243438.CDS1.S1_s_at telomerase RNA, v-TR (MDV001) 179.63 63.39 786.73 762.29 0.35 4.38 4.24

AF243438.CDS10.S1_s_at R-LORF14, 24 KD phosphoprotein, pp24

(MDV008)

32.94 882.14 440.84 26.78 13.38

AF243438.CDS11.S1_s_at lipase, v-LIP (MDV010) 907.47 411.86 10438.66 10210.69 0.45 11.50 11.25

AF243438.CDS3.S1_s_at CxC chemokine, v-IL8 (MDV003) 443.00 161.26 11761.70 7149.10 0.36 26.55 16.14

AF243438.CDS4.S1_s_at Meq, MEQ protein (MDV005) 305.30 235.18

AF243438.CDS55.S1_s_at UL41, virion host shutoff protein-like protein

(MDV054)

29.33 428.39 259.50 14.61 8.85

AF243438.CDS64.S1_s_at UL49.5, envelope/tegument protein-like

protein (MDV064)

26.70 48.41 40.01 34.16 1.81 1.50 1.28

AF243438.CDS74.S1_s_at R-LORF14A, 38 KD phosphoprotein, pp38

(MDV073)

238.59 82.82 2053.42 1714.56 0.35 8.61 7.19

AF243438.CDS85.S1_s_at RS1, immediate-early gene transactivator

ICP4-like protein (MDV084)

233.98 294.31

AF243438.CDS86.S1_s_at antisense RNA protein /NOTE = similar to

HSV1 RS1 immediate-early gene

transactivator ICP4 (MDV083)

107.83 134.86 5185.46 2292.14 1.25 48.09 21.26

AF243438.CDS94.S1_s_at US3, serine threonine protein kinase-like

protein (MDV092)

215.38

AF243438.CDS95.S1_s_at MDV1 S3 /NOTE = similar to HSV1 US10

virion protein (MDV093)

246.10 93.27

NC-002229.CDS4.S1_s_at RLORF4 169.12 199.24

Virus replication

AF243438.CDS21.S1_s_at UL8, DNA helicase-primase associated

protein-like protein (MDV020)

651.20 369.63

AF243438.CDS22.S1_s_at UL9, ori binding protein-like protein

(MDV021)

164.84

AF243438.CDS25.S1_s_at UL12, DNase-like protein (MDV024) 196.33 3162.80 2169.80 16.11 11.05

AF243438.CDS28.S1_s_at UL15, DNA packaging protein-like protein

(MDV027)

48.53 637.63 361.08 13.14 7.44

AF243438.CDS36.S1_s_at UL23, thymidine kinase-like protein

(MDV036)

195.53 72.71


(MDV041)

94.26

AF243438.CDS43.S1_s_at UL29, single stranded DNA binding protein-

like protein (MDV042)

148.17 2264.39 1635.39 15.28 11.04

AF243438.CDS44.S1_s_at UL30, DNA polymerase catalytic subunit-like

protein (MDV043)

688.12 420.70


(MDV046)

259.15 274.16

AF243438.CDS53.S1_s_at UL39, ribonucleotide reductase large subunit-


37.50 211.10 174.80 5.63 4.66

AF243438.CDS54.S1_s_at UL40, ribonucleotide reductase large subunit-


478.96 121.56 8152.52 5990.39 0.25 17.02 12.51

AF243438.CDS56.S1_s_at UL42, DNA polymerase processivity subunit-


10.34 54.12 552.26 356.11 5.23 53.41 34.44

AF243438.CDS62.S1_s_at UL48, gene transactivator-like protein

(MDV061)

199.22 68.99 2786.31 2781.22 0.35 13.99 13.96

AF243438.CDS65.S1_s_at UL50, dUTPase-like protein (MDV063) 284.86 110.78 4305.87 3285.40 0.39 15.12 11.53

1788 X. Hu et al.

123

Table 1 continued



I7

I21/

I7

I28/

I7

AF243438.CDS67.S1_s_at UL52, DNA helicase/primase-like protein

associated protein (MDV066)

131.02

AF243438.CDS69.S1_s_at UL54, post translational gene regulation,

ICP27 (MDV068)

202.92 82.27 4266.16 2721.33 0.41 21.02 13.41

AF243438.CDS90.S1_s_at US1, phosphoprotein ICP22-like protein

(MDV088)

60.02 24.45 885.68 772.86 0.41 14.76 12.88

Tegument

AF243438.CDS24.S1_s_at UL11, myristylated tegument protein-like

protein (MDV023)

425.07 87.55 9631.05 4232.90 0.21 22.66 9.96

AF243438.CDS27.S1_s_at UL14, minor tegument protein-like protein

(MDV026)

69.90 16.12 2176.73 980.70 0.23 31.14 14.03

AF243438.CDS34.S1_s_at UL21, tegument protein-like protein

(MDV033)

569.40 319.09

AF243438.CDS50.S1_s_at UL36, large tegument protein-like protein

(MDV049)

598.47 438.39

AF243438.CDS51.S1_s_at UL37, tegument protein-like protein

(MDV050)

134.77

AF243438.CDS60.S1_s_at UL46, tegument phosphoprotein-like protein

(MDV059)

202.64 164.65 2883.70 2594.08 0.81 14.23 12.80


(MDV060)

87.86


(MDV062)

30.89 248.63 211.49

Glycoprotein

AF243438.CDS23.S1_s_at UL10, viron membrane glycoprotein M-like

protein (MDV022)

1125.52 708.63

AF243438.CDS35.S1_s_at UL22, envelope glycoprotein H-like protein

(MDV034)

165.00 2418.72 1504.01 14.66 9.12

AF243438.CDS41.S1_s_at UL27, virion membrane glycoprotein B-like

protein (MDV040)

214.30 84.80 3029.93 1975.15 0.40 14.14 9.22

AF243438.CDS58.S1_s_at UL44, virion membrane glycoprotein C-like

protein (MDV057)

169.63 1841.71 1191.04 10.86 7.02

AF243438.CDS68.S1_s_at UL53, glycoprotein K-like protein (MDV067) 102.44

AF243438.CDS96.S1_s_at US6, membrane glycoprotein D-like protein

(MDV094)

172.22 67.06

AF243438.CDS97.S1_s_at US7, membrane glycoprotein I-like protein

(MDV095)

236.88

AF243438.CDS98.S1_s_at US8, membrane glycoprotein E-like protein

(MDV096)

314.91 92.73 5410.26 3746.48 0.29 17.18 11.90

AF243438.CDS99.S1_at N-terminus MDV1 S2 /NOTE = similar to

HSV1 US8 membrane glycoprotein E

(MDV097)

46.11 61.01 1150.55 452.49 1.32 24.95 9.81

AF243438.CDS99.S1_s_at N-terminus MDV1 S2 /NOTE = similar to

HSV1 US8 membrane glycoprotein E

(MDV097)

51.32

NC-002229.CDS44.S1_s_at UL26 /NOTE = gH; forms a complex with

UL1 gene product glycoprotein L (MDV038)

1759.24 1038.86

NC-002229.CDS82.S1_at LORF12 /NOTE = gC 122.31 1853.55 741.78 15.15 6.06

Nucleocapsid

AF243438.CDS16.S1_s_at UL3, nuclear phosphoprotein-like protein

(MDV015)

79.05 623.19 597.15 7.88 7.55

Transcription of Marek’s disease virus genes in thymus 1789

123

Table 1 continued



I7

I21/

I7

I28/

I7

AF243438.CDS17.S1_s_at UL4, nuclear protein-like protein (MDV016) 324.51 304.36

AF243438.CDS19.S1_s_at UL6, minor capsid protein-like protein

(MDV018)

80.18

AF243438.CDS31.S1_s_at UL18, nucleocapsid protein-like protein

(MDV030)

236.11 78.89 3682.05 3398.90 0.33 15.59 14.40

AF243438.CDS32.S1_s_at UL19, major capsid protein-like protein

(MDV031)

95.83 112.18

AF243438.CDS45.S1_s_at UL31, nuclear phosphoprotein-like protein

(MDV044)

404.82 101.93 3032.19 2167.07 0.25 7.49 5.35

AF243438.CDS49.S1_s_at UL35, capsid protein-like protein (MDV048) 303.58 132.60 13815.84 5920.17 0.44 45.51 19.50

AF243438.CDS52.S1_s_at UL38, capsid protein-like protein (MDV051) 84.90 1114.99 713.63 13.13 8.41

Other protein

AF243438.CDS20.S1_s_at UL7-like protein (MDV019) 522.23 357.91

AF243438.CDS33.S1_s_at UL20, transmembrane protein-like protein,

virus egress (MDV032)

147.20

AF243438.CDS48.S1_s_at UL34, membrane phosphoprotein-like protein

(MDV047)

5.23 16.72 300.14 326.11 3.20 57.39 62.36

AF243438.CDS57.S1_s_at UL43, probable membrane protein (MDV056) 144.38 47.19 3757.73 2665.30 0.33 26.03 18.46

AF243438.CDS59.S1_s_at UL45, envelope/transmembrane protein-like

protein, cell fusion (MDV058)

222.32 140.97

AF243438.CDS6.S1_s_at 14 KD lytic phase protein (MDV006) 139.30 68.06 2313.77 1585.84 0.49 16.61 11.38

AF243438.CDS66.S1_s_at UL51, virion phophoprotein-like protein

(MDV065)

59.70 1129.77 678.63

AF243438.CDS71.S1_s_at UL55-like protein (MDV070) 283.48 120.30 10742.49 5078.38 0.42 37.89 17.91

AF243438.CDS88.S1_s_at Cytoplasmic protein (MDV086) 124.74 171.99 6823.98 4938.32 1.38 54.70 39.59

AF243438.CDS91.S1_s_at US10, virion protein-like protein (MDV089) 488.61 231.58 6902.77 6305.32 0.47 14.13 12.90

AF243438.CDS92.S1_s_at MDV1 S3 /NOTE = similar to HSV1 US10

virion protein (MDV090)

43.32 779.93 463.01 18.00 10.69

NC-002229.CDS5.S1_s_at RLORF5 49.73 753.05 356.54

Hypothetical protein

AF243438.CDS12.S1_s_at hypothetical protein (MDV011) 147.21 132.34

AF243438.CDS13.S1_s_at LORF2, hypothetical protein (MDV012) 95.17 34.09 2564.81 1884.26 0.36 26.95 19.80

AF243438.CDS70.S1_s_at LORF4, hypothetical protein (MDV069) 2437.13 1337.72

AF243438.CDS72.S1_s_at hypothetical protein (MDV071) 41.06 47.60 478.38 367.03 1.16 11.65 8.94

AF243438.CDS8.S1_s_at RLORF12, hypothetical protein (MDV007) 270.23 184.14 2238.32 875.33 0.68 8.28 3.24

AF243438.CDS83.S1_s_at hypothetical protein (MDV081) 57.12 950.27 480.86

AF243438.CDS84.S1_s_at hypothetical protein (MDV082) 242.28 187.69 5826.73 3865.89 0.77 24.05 15.96



AY510475.CDS10.S1_s_at RLORF11, hypothetical protein 131.75 132.14 3928.20 1923.82 1.00 29.82 14.60

AY510475.CDS3.S1_at USex1, hypothetical protein 41.35 77.39 116.28 1.87 2.81

AY510475.CDS45.S1_s_at LORF5, hypothetical protein 578.78 149.27

AY510475.CDS6.S1_s_at RLORF3, hypothetical protein 197.39

AY510475.CDS8.S1_s_at RLORF8, hypothetical protein 103.01

AY510475.CDS81.S1_s_at UL56, hypothetical protein 425.04 323.75 8350.26 5519.40 0.76 19.65 12.99

AY510475.CDS87.S1_s_at UL56, hypothetical protein 1089.00 356.96 16885.68 9402.15 0.33 15.51 8.63

1790 X. Hu et al.

123

all carried out at Shanghai Biotechnology Corporation. The

raw data were normalised using the MAS 5.0 algorithm,

Gene Spring Software 11.0 (Agilent Technologies, Santa

Clara, CA, USA).

An uninfected chicken thymus was used as a control,

and RNA samples from control birds were used for

detection of background signal intensity (noise) in the

microarray analysis.

The kinetics of expression profiling of MDV transcripts

in infected chicken thymus tissues showed that a total of 86

MDV genes (7 dpi, 47; 14 dpi, 39; 21 dpi, 80; and 28 dpi,

78) were detected, but no MDV gene was found in

control thymus tissues (Table 1). At 7 dpi, 47 MDV gene

transcripts were found. These genes mainly encoded the

virion membrane glycoprotein, envelope glycoprotein,

capsid protein, DNA packaging protein and nucleocapsid

protein. Expression of most of these genes was increased at

21 and 28 dpi but reduced or shut down at 14 dpi. This

result indicated that a latent infection was established at

14 dpi in the thymus infected with the RB1B strain. Only

37 MDV transcripts were detected at this stage, and their

relative abundance was very low.

Seventeen genes associated with virus replication were

detected in infected thymus (Table 1; Fig. 1A). These virus

genes mainly encoded DNA helicase-primase associated

protein, ori-binding protein, single-stranded DNA binding

Fig. 1 Kinetics of expression of MDV transcripts involved in virus replication (A) and immune evasion and/or tumor development (C) and

those encoding glycoproteins (B) and tegument proteins (D) in thymus infected with the RB1B strain

Table 1 continued



I7

I21/

I7

I28/

I7

AY510475.CDS9.S1_s_at RLORF10, hypothetical protein 867.18 391.36

Relative expression level = relative expression level of MDV genes in infected chicken thymus by microarray analysis

I14/I7 = 14 dpi/7 dpi. Fold change [1, genes that were upregulated at 14 dpi in comparison to 7 dpi; fold change \1, genes that were

downregulated at 14 dpi in comparison to 7 dpi. Fold change = 1, genes with no change in the expression levels between 14 and 7 dpi

I21/I7 = 21 dpi/7 dpi. Fold change [ 1, genes that were upregulated at 21 dpi in comparison to 7 dpi

I28/I7 = 28 dpi/7 dpi. Fold change [1, genes that were upregulated at 28 dpi in comparison to 7 dpi


123

protein, DNA packaging protein, ribonucleotide reductase

protein, DNA polymerase processivity subunit-like protein

and posttranslational gene regulation. Expression of these

genes, with the exception of UL42 (encoding DNA poly-

merase processivity subunit-like protein), was reduced or

shut down at 14 dpi but increased sharply at 21 and 28 dpi.

In addition, 12 MDV genes encoding glycoproteins were

detected in infected thymus. However only gB and gE were

detected at 14 dpi (Table 1; Fig. 1B). The relative abun-

dance of gB, an important MDV gene that represents the

level of virus replication, was reduced from 214.30 at 7 dpi

to 84.80 at 14 dpi, then increased to 3029.93 at 21 dpi and

1975.15 at 28 dpi. The abundance of gE was reduced from

314.91 at 7 dpi to 92.73 at 14 dpi, then increased to

5410.26 and 3746.48 at 21 and 28 dpi, respectively. The

results indicate that a latent infection was established at 14

dpi in the thymus infected with RB1B strain.

Thirteen genes involved in immune evasion and/or

tumour development were detected in infected thymus

(Table 1; Fig. 1C). These genes included UL49.5, UL41,

US3, Meq, v-TR, v-IL8, v-LIP, RLORF4, pp24, pp38,

RS1, MDV1 S3 and antisense RNA. From the kinetics of

expression profiling of these genes, we also found that the

expression of these genes was restricted at 14 dpi, and they

were over-activated at 21 and 28 dpi in infected thymus

(Fig. 1C). Only one of them, UL49.5, was increased at 14

dpi, and it showed similar abundance at 21 and 28 dpi.

UL49.5 is involved in the downregulation of MHC class I

molecules in MDV-infected cells [11].

In addition, eight viral genes encoding tegument pro-

teins (UL11, UL14, UL21, UL36, UL37, UL46, UL47 and

UL49) were detected in our experiment (Table 1; Fig. 1D).

For herpes simplex virus type 1 (HSV-1), UL14 not only

blocks apoptosis (both Meq and vTR have anti-apoptotic

properties) but also possesses heat shock protein (HSP)-

like functions and regulates viral replication [15, 16]. In

our previous research, we found that the expression of

HSP90 protein was reduced after MDV infection [9]. It is

recognized that HSP90 plays an important role not only in

the folding and stability of many carcinogenic signalling

proteins but also during herpes simplex virus infection and

replication [3, 12]. In this case, UL14 could function in

MDV replication and transformation. We speculate that

UL14 could be a previously unrecognized viral oncogene

and have been studying the function of UL14.

To confirm the microarray results, real-time PCR was

performed on four selected genes (gB, Meq, vTR and

UL14) as reported previously [9]. The sequences of the

primers are given in Electronic Supplementary Material;

the sequences for the primers for 18S and Meq were

reported previously [1, 13]. Gene expression levels were

normalised against the expression of chicken 18S mRNA

and data were compared using Student’s t-test with the

Statistical Package for Social Sciences (version 16.0).

Table 2 shows the relative differences in expression of

selected MDV genes based on real-time PCR results. The

expression levels of gB and UL14 were transiently

increased at 7 dpi and decreased at 14 dpi, then increased

again at 21 dpi and decreased at 28 dpi. The corresponding

changes were also observed in the array results. However,

the expression of vTR and Meq was not fully in agreement

with the array results. This discrepancy, which has been

Table 2 MDV gene expression analysis by real-time PCR

Gene Days postinfection Cn mean ± SD DCn mean DCn SE Relative expression Fold difference

gB 7 33.53 ± 0.23 18.73 0.14 168.96 1.00

gB 14 35.50 ± 0.34 21.80 0.17 27.98 0.17

gB 21 31.03 ± 0.30 15.93 0.17 7067.23 41.83

gB 28 31.51 ± 0.24 16.99 0.12 2526.04 14.95

Meq 7 30.87 ± 0.14 16.07 0.08 2710.44 1.00

Meq 14 29.08 ± 0.10 15.38 0.05 1965.94 0.73

Meq 21 26.02 ± 0.18 10.92 0.12 236108.52 87.11

Meq 28 25.89 ± 0.09 11.38 0.06 146853.16 54.18

UL14 7 27.68 ± 0.07 12.89 0.06 899.26 1.00

UL14 14 29.63 ± 0.33 15.94 0.19 11.95 0.01

UL14 21 27.95 ± 0.09 13.43 0.06 2473.06 2.75

UL14 28 28.95 ± 0.05 13.84 0.08 888.78 0.99

vTR 7 30.73 ± 0.21 15.93 0.12 13.26 1.00

vTR 14 28.58 ± 0.24 14.89 0.12 32.58 2.46

vTR 21 27.78 ± 0.23 12.68 0.14 230.65 17.39

vTR 28 28.29 ± 0.13 13.77 0.07 21.28 1.61

1792 X. Hu et al.

123

observed previously [5], may reflect developmental chan-

ges in vTR and Meq gene expression or mRNA stability.

In conclusion, we provide an expression profile of MDV

transcripts and kinetics of expression of MDV transcripts in

the thymus of chickens. A total of 86 MDV genes were

detected in infected chicken thymus. The data may provide

the groundwork for future investigation into the biology

and pathogenesis of MDV.

Acknowledgments This research was supported by the National

Natural Science Foundation of China (30871873, 31072135), Major

Basic Research of Natural Science Foundation of the Jiangsu Higher

Education Institutions of China (Grant No. 12KJA23001) and The

Program for Changjiang Scholars and Innovative Research Team in

University (IRT0978).

References

1. Abdul-Careem MF, Hunter BD, Nagy E, Read LR, Sanei B,

Spencer JL, Sharif S (2006) Development of a real-time PCR

assay using SYBR Green chemistry for monitoring Marek’s

disease virus genome load in feather tips. J Virol Methods

133:34–40

2. Biggs PM (2001) The history and biology of Marek’s disease

virus. Curr Topics Microbiol Immunol 255:1–24

3. Burch AD, Weller SK (2005) Herpes simplex virus type 1 DNA

polymerase requires the mammalian chaperone hsp90 for proper

localization to the nucleus. J Virol 79:10740–10749

4. Cantello JL, Anderson AS, Morgan RW (1994) Identification of

latency-associated transcripts that map antisense to the ICP4

homolog gene of Marek’s disease virus. J Virol 68:6280–6290

5. Goh SH, Josleyn M, Lee YT, Danner RL, Gherman RB, Cam

MC, Miller JL (2007) The human reticulocyte transcriptome.

Physiol Genomics 30:172–178

6. Haq K, Brisbin JT, Thanthrige-Don N, Heidari M, Sharif S

(2010) Transcriptome and proteome profiling of host responses to

Marek’s disease virus in chickens. Vet Immunol Immunopathol

138:292–302

7. Heidari M, Huebner M, Kireev D, Silva RF (2008) Transcrip-

tional profiling of Marek’s disease virus genes during cytolytic

and latent infection. Virus Genes 36:383–392

8. Heidari M, Sarson AJ, Huebner M, Sharif S, Kireev D, Zhou H

(2010) Marek’s disease virus-induced immunosuppression: array

analysis of chicken immune response gene expression profiling.

Viral Immunol 23:309–319

9. Hu X, Qin A, Qian K, Shao H, Yu C, Xu W, Miao J (2012)

Analysis of protein expression profiles in the thymus of chickens

infected with Marek’s disease virus. Virology J 9:256

10. Jarosinski KW, Tischer BK, Trapp S, Osterrieder N (2006)

Marek’s disease virus: lytic replication, oncogenesis and control.

Expert Rev Vaccines 5:761–772

11. Jarosinski KW, Hunt HD, Osterrieder N (2010) Down-regulation

of MHC class I by the Marek’s disease virus (MDV) UL49.5 gene

product mildly affects virulence in a haplotype-specific fashion.

Virology 405:457–463

12. Li YH, Tao PZ, Liu YZ, Jiang JD (2004) Geldanamycin, a ligand

of heat shock protein 90, inhibits the replication of herpes sim-

plex virus type 1 in vitro. Antimicrob Agents Chemother

48:867–872

13. Li YP, Bang DD, Handberg KJ, Jorgensen PH, Zhang MF (2005)

Evaluation of the suitability of six host genes as internal control

in real-time RT-PCR assays in chicken embryo cell cultures

infected with infectious bursal disease virus. Vet Microbiol

110:155–165

14. Lu ZJ, Qin AJ, Qian K, Chen XH, Jin WJ, Zhu YF, Eltahir YM

(2010) Proteomic analysis of the host response in the bursa of

Fabricius of chickens infected with Marek’s disease virus. Virus

Res 153:250–257

15. Yamauchi Y, Wada K, Goshima F, Daikoku T, Ohtsuka K, Ni-

shiyama Y (2002) Herpes simplex virus type 2 UL14 gene

product has heat shock protein (HSP)-like functions. J Cell Sci

115:2517–2527

16. Yamauchi Y, Daikoku T, Goshima F, Nishiyama Y (2003) Her-

pes simplex virus UL14 protein blocks apoptosis. Microbiol

Immunol 47:685–689


123

transcriptional profile of marek’s disease virus genes in chicken thymus during different phases...

Documents